The DOI matches its Crossref record; 36 of the 38 references it cites were found in a registry or an index.
A Protein-Counting Mechanism for Telomere Length Regulation in Yeast
Open accessAbstract
In the yeast Saccharomyces cerevisiae , telomere elongation is negatively regulated by the telomere repeat-binding protein Rap1p, such that a narrow length distribution of telomere repeat tracts is observed. This length regulation was shown to function independently of the orientation of the telomere repeats. The number of repeats at an individual telomere was reduced when hybrid proteins containing the Rap1p carboxyl terminus were targeted there by a heterologous DNA-binding domain. The extent of this telomere tract shortening was proportional to the number of targeted molecules, consistent with a feedback mechanism of telomere length regulation that can discriminate the precise number of Rap1p molecules bound to the chromosome end.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“However, a strong common theme that has emerged is the likely involvement of a protein-counting mechanism in both systems (31, 44).”
From Control of Human Telomere Length by TRF1 and TRF2 (2000) · cites this paper as [31]
Citations
Cites
Identification of a specific telomere terminal transferase activity in tetrahymena extracts
Greider, C. W., & Blackburn, E. H. (1985) · Cell · doi:10.1016/0092-8674(85)90170-9 · Cited by 3,400
WATSON, J. D. (1972) · Nature New Biology · doi:10.1038/newbio239197a0 · Cited by 1,632
Position effect at S. cerevisiae telomeres: Reversible repression of Pol II transcription
Gottschling, D. E., Aparicio, O. M., Billington, B. L., & Zakian, V. A. (1990) · Cell · doi:10.1016/0092-8674(90)90141-z · Cited by 1,325
Greider, C. W. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.002005 · Cited by 1,032
Telomeres: Beginning to Understand the End
Zakian, V. A. (1995) · Science · doi:10.1126/science.270.5242.1601 · Cited by 859
TLC1 : Template RNA Component of Saccharomyces cerevisiae Telomerase
Singer, M. S., & Gottschling, D. E. (1994) · Science · doi:10.1126/science.7545955 · Cited by 736
Chong, L., van Steensel, B., Broccoli, D., Erdjument‐Bromage, H., Hanish, J., Tempst, P., & de Lange, T. (1995) · Science · doi:10.1126/science.270.5242.1663 · Cited by 714
Cdc13p: A Single-Strand Telomeric DNA-Binding Protein with a Dual Role in Yeast Telomere Maintenance
Nugent, C. I., Hughes, T., Lue, N. F., & Lundblad, V. (1996) · Science · doi:10.1126/science.274.5285.249 · Cited by 606
Moretti, P. M., Freeman, K., Coodly, L. R., & Shore, D. (1994) · Genes & Development · doi:10.1101/gad.8.19.2257 · Cited by 547
Self-citationYUDKIN, J. (1972) · Nature · doi:10.1038/239197a0 · Cited by 545
Flagged first, then by citations
2 of the 38 references couldn’t be matched to a known paper.
Research works printed but not linked: 11
- ibid. 51, 887 (1987);
- Harley C. B., Telomeres,, Blackburn E., Greider C., Eds. (Cold Spring Harbor Press, Plainview, NY, 1995247-263).
- Lustig A. J. and , Petes T. D., ibid. 83, 1398 (1986).
- Krauskopf A. and , Blackburn E. H., ibid. 383, 354 (1996);
- Buck S. thesis Columbia University (1996).
- Kyrion G., Boakye K. A., Lustig A. J., Mol. Cell. Biol. 12, 5159 (1992).
- Overexpression of the COOH-terminal half of Rap1p from a high-copy number plasmid was reported to cause telomere lengthening (5) [C. F. J. Hardy thesis Columbia University (1991)]. In our experiments the Gbd/Rap1 hybrid was expressed on a centromere plasmid by means of the RAP1 promoter which most likely explains its lack of effect on telomere length in the absence of UAS G sites.
- Chien C.-T., Buck S., Sternglanz R., Shore D., ibid.531.
- Grandin N. , Reed S. I. , Charbonneau M., Genes Dev., in press.
- Wotton D. and , Shore D., ibid., in press.
- van Steensel B. de Lange T. Nature in press.
Cited by
Sorted by citations
Items 201–300 of 522
Telomerase activity and telomere length in benign and malignant human thyroid tissues
Kammori, M. (2000) · Cancer Letters · doi:10.1016/s0304-3835(00)00547-4 · Cited by 57
Crisis intervention: The role of telomerase
Lustig, A. J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3339 · Cited by 61
Rap1p telomere association is not required for mitotic stability of a C3TA2 telomere in yeast
Alexander, M. K., & Zakian, V. A. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg154 · Cited by 56
The number of vertebrate repeats can be regulated at yeast telomeres by Rap1‐independent mechanisms
Brevet, V., Berthiau, A., Civitelli, L., Donini, P., Schramke, V., Géli, V., Ascenzioni, F., & Gilson, É. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg155 · Cited by 57
Telomere length inheritance and aging
Kappei, D., & Londoño‐Vallejo, A. (2007) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2007.10.009 · Cited by 57
The MRX Complex Plays Multiple Functions in Resection of Yku- and Rif2-Protected DNA Ends
Bonetti, D., Clerici, M., Manfrini, N., Lucchini, G., & Longhese, M. P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0014142 · Cited by 55
“Conversely, telomerase action is negatively regulated by Rap1, Rif1 and Rif2 [12,13], which bind telomeric double-stranded DNA and also inhibit NHEJ at telomeres [14].”
BackgroundCulture Models of Human Mammary Epithelial Cell Transformation
Stampfer, M. R., & Yaswen, P. (2000) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1023/a:1009525827514 · Cited by 54
“Once telomerase has been reactivated, a mechanism exists to maintain telomere length within a stable range, perhaps similar to mechanisms that maintain stable telomere lengths in unicellular organisms such as yeast (68).”
Taz1 Binding to a Fission Yeast Model Telomere
Tomáška, Ľ., Willcox, S., Slezakova, J., Nosek, J., & Griffith, J. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409790200 · Cited by 58
MRX-dependent DNA Damage Response to Short Telomeres
Viscardi, V., Bonetti, D., Cartagena‐Lirola, H., Lucchini, G., & Longhese, M. P. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-03-0285 · Cited by 53
“…mechanism takes into account also the additional 270 bp blocks of TG1–3 telomeric repeats, which are present in single (TEL270) or double copy (2 TEL270) between the URA3 gene and the telomere-proximal Flp1 site in strains Lev189 and Lev220, respectively (Marcand et al., 1997; Figure 5A).”
Subtelomeric factors antagonize telomere anchoring and Tel1‐independent telomere length regulation
Hediger, F., Berthiau, A.-S., Houwe, G. V., Gilson, É., & Gasser, S. M. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600976 · Cited by 53
“The number of Rap1/Rif1-2 complexes bound to telomeric DNA negatively regulates telomerase by reducing the probability that it will elongate the TG(1 3) repeat (Marcand et al, 1997; Levy and Blackburn, 2004; Teixeira et al, 2004).”
Chappell, A. S., & Lundblad, V. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.17.7720-7736.2004 · Cited by 55
“At fully replicated telomeres, telomerase accessibility to chromosome termini is inhibited, in cis, by proteins bound to the duplex telomeric tract RNP (1, 34, 38, 39 , 51).”
BackgroundProtecting the terminus: t-loops and telomere end-binding proteins
Wei, C., & Price, C. M. (2003) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-3244-z · Cited by 53
Telomere transitions in yeast: the end of the chromosome as we know it
Cooper, J. P. (2000) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(00)00070-8 · Cited by 55
Liu, Z., Dominy, B. N., & Shakhnovich, E. I. (2004) · Journal of the American Chemical Society · doi:10.1021/ja032018q · Cited by 52
Telomerase: Dr Jekyll or Mr Hyde?
Prescott, J. C., & Blackburn, E. H. (1999) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(99)80055-0 · Cited by 52
Cdc13 subcomplexes regulate multiple telomere functions.
Lustig, A. J. (2001) · Nature Structural Biology · doi:10.1038/86157 · Cited by 52
Rap1P and Telomere Length Regulation in Yeast
Marcand, S., Wotton, D., Gilson, É., & Shore, D. (2007) · Novartis Foundation symposium · doi:10.1002/9780470515433.ch6 · Cited by 55
Self-citationSerakıncı, N., Christensen, R., Graakjær, J., Cairney, C. J., Keith, W. N., Alsner, J., Saretzki, G. C., & Kølvraa, S. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.01.002 · Cited by 52
“Furthermore, it has been indicated that longer telomeres are more likely to rebuild the cap than are shorter telomeres [32,33].”
BackgroundOrganization of Chromosome Ends in Ustilago maydis. RecQ-like Helicase Motifs at Telomeric Regions
Alonso, P. S., & Guzmán, P. (1998) · Genetics · doi:10.1093/genetics/148.3.1043 · Cited by 50
Telomere length maintenance in aging and carcinogenesis.
Aragona, M., Maisano, R., Panetta, S., Giudice, A., Morelli, M., Torre, I. L., & Torre, F. L. (2000) · International Journal of Oncology · doi:10.3892/ijo.17.5.981 · Cited by 51
Denisenko, O. N., & Bomsztyk, K. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.1.286-297.2002 · Cited by 50
Composition and conservation of the telomeric complex
Kanoh, J., & Ishikawa, F. (2003) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-3245-y · Cited by 50
Telomeres: Influencing the Rate of Aging
von Zglinicki, T. (1998) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1998.tb09912.x · Cited by 48
Induction of Telomerase Activity by Irradiation in Human Lymphoblasts
Neuhof, D., Ruess, A., Wenz, F. K., & Weber, K. J. (2001) · Radiation Research · doi:10.1667/0033-7587(2001)155[0693:iotabi]2.0.co;2 · Cited by 49
“Studies in yeast and human cells indicate that cells count telomere-binding proteins to determine their telomere length (34, 35).”
BackgroundPrescott, J. C., & Blackburn, E. H. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.8.2941-2948.2000 · Cited by 51
“It has been proposed that normally, two mutually reinforcing telomeric components contribute to length control: a proper regulatory end structure that is disrupted upon incorporation of mutant residues into the terminal telomeric repeat(s); and a higher-order structure, destabilized by telomere shortening, that normal…”
BackgroundProteins that bind to double-stranded regions of telomeric DNA
Brun, C., Marcand, S., & Gilson, É. (1997) · Trends in Cell Biology · doi:10.1016/s0962-8924(97)01092-1 · Cited by 49
Self-citationPyrogallol-Based Molecules as Potent Inhibitors of the Antiapoptotic Bcl-2 Proteins
Tang, G., Yang, C., Nikolovska‐Coleska, Z., Guo, J., Qiu, S., Wang, R., Gao, W., Wang, G., Stuckey, J. A., Krajewski, K., et al. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm061400l · Cited by 48
In Vivo Analysis of Functional Regions within Yeast Rap1p
Graham, I. R., Haw, R., Spink, K. G., Halden, K. A., & Chambers, A. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.11.7481 · Cited by 48
“Rap1p is a yeast multifunctional protein involved in transcriptional activation, transcriptional silencing, and telomere function (13, 29, 30, 34, 35, 46, 47).”
BackgroundInvolvement of Topoisomerase III in Telomere-Telomere Recombination
Tsai, H.-J., Huang, W., Li, T., Tsai, Y.-L., Wu, K., Tseng, S., & Teng, S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600649200 · Cited by 49
Telomere Length Influences Cancer Cell Differentiation In Vivo
Hirashima, K., Migita, T., Sato, S., Muramatsu, Y., Ishikawa, Y., & Seimiya, H. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00136-13 · Cited by 50
“In general, telomere length in telomerase-positive cells is regulated by the “protein-counting” mechanism, in which longer telomeres contain higher levels of shelterin and therefore block the access of telomerase more intensely (8).”
BackgroundLin, C., Chang, H.-H., Wu, K., Tseng, S., Lin, C., Lin, C., & Teng, S. (2005) · Eukaryotic Cell · doi:10.1128/ec.4.2.327-336.2005 · Cited by 52
“The copy number of the Rap1p complex negatively regulates telomere length (24, 47).”
BackgroundHumanizing the yeast telomerase template
Henning, K. A., Moskowitz, N. H., Ashlock, M. A., & Liu, P. P. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.10.5667 · Cited by 47
Soohoo, C., Shi, R., Lee, T. H., Huang, P., Lu, K. P., & Zhou, X. Z. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.180174 · Cited by 47
Early Gene Expression Profile in Mouse Brain after Exposure to Ionizing Radiation
Mahmoud-Ahmed, A. S., Atkinson, S., & Wong, C. S. (2006) · Radiation Research · doi:10.1667/rr3485.1 · Cited by 47
“Terf1 was proposed to play a role in regulating telomere length (41), and there is evidence that Terf1 expression has a prognostic role in adrenal tumors (42).”
BackgroundThe finger subdomain of yeast telomerase cooperates with Pif1p to limit telomere elongation
Eugster, A., Lanzuolo, C., Bonneton, M., Luciano, P., Pollice, A., Pulitzer, J. F., Stegberg, E., Berthiau, A.-S., Förstemann, K., Corda, Y., et al. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1126 · Cited by 45
A tale of the good and bad: Cell senescence in bone homeostasis and disease
Liu, X., & Wan, M. (2019) · International review of cytology · doi:10.1016/bs.ircmb.2019.03.005 · Cited by 45
Telomere length measurement by Q-FISH
Slijepčević, P. (2001) · Methods in Cell Science · doi:10.1023/a:1013177128297 · Cited by 44
Jun, H.-I., Liu, J., Jeong, H., Kim, J., & Qiao, F. (2013) · Genes & Development · doi:10.1101/gad.219485.113 · Cited by 47
Rodrigo, G., Carrera, J., & Jaramillo, A. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr616 · Cited by 44
Protection against chromosome degradation at the telomeres
Grandin, N., & Charbonneau, M. (2007) · Biochimie · doi:10.1016/j.biochi.2007.07.008 · Cited by 45
Nakamura, M., Nabetani, A., Mizuno, T., Hanaoka, F., & Ishikawa, F. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.24.11073-11088.2005 · Cited by 44
“binding proteins (TRF1 in vertebrates) (41, 62).”
Varying the number of telomere-bound proteins does not alter telomere length in tel1Δ cells
Ray, A., & Runge, K. W. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.26.15044 · Cited by 43
Tang, G., Ding, K., Nikolovska‐Coleska, Z., Yang, C., Qiu, S., Shangary, S. K., Wang, R., Guo, J., Gao, W., Meagher, J. L., et al. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm070383c · Cited by 42
Multiple POT1–TPP1 Proteins Coat and Compact Long Telomeric Single-Stranded DNA
Taylor, D. J., Podell, E. R., Taatjes, D. J., & Cech, T. R. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.04.049 · Cited by 44
Characterization of Protein−Ligand Interactions by High-Resolution Solid-State NMR Spectroscopy
Zech, S. G., Olejniczak, E. T., Hajduk, P. J., Mack, J. C., & McDermott, A. E. (2004) · Journal of the American Chemical Society · doi:10.1021/ja040086m · Cited by 42
Taylor, H. O. B., O’Reilly, M., Leslie, A. G. W., & Rhodes, D. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4161 · Cited by 43
Theme and Variation Among Silencing Proteins in Saccharomyces cerevisiae and Kluyveromyces lactis
Åström, S. U., & Rine, J. (1998) · Genetics · doi:10.1093/genetics/148.3.1021 · Cited by 41
Telomerase-Independent Stabilization of Short Telomeres in Trypanosoma brucei
Dreesen, O., & Cross, G. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00212-06 · Cited by 41
“The ability of telomerase to extend a telomere is inversely proportional to the initial length of the telomere DNA repeats (36, 37, 56).”
BackgroundMethodGrossi, S., Bianchi, A., Damay, P., & Shore, D. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.23.8117-8128.2001 · Cited by 44
“Our results extend previous work (34, 45, 46) by demonstrating a”
BackgroundResultInfluentialSelf-citationDomenico, E. G. D., Romano, E., Porto, P. D., & Ascenzioni, F. (2014) · BioMed Research International · doi:10.1155/2014/787404 · Cited by 39
“According to the counting model, as telomeres get shorter, the number of Rap1-Rif2 molecules decreases [171, 172] and elicits the signal for MRX and Tel1 and ultimately telomerase recruitment.”
Tomita, K. (2018) · Current Genetics · doi:10.1007/s00294-018-0836-6 · Cited by 43
“Hence, I predict that accumulation of the Pot1 complex on the synthesised telomere G-strand DNA serves to release telomerase, reminiscent of the classic counting mechanism (Marcand et al. 1997).”
Yu, E. Y., Yen, W.-F., Steinberg‐Neifach, O., & Lue, N. F. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00986-09 · Cited by 40
“cerevisiae telomeres, Rap1 has been demonstrated to serve at least two critical functions: suppressing telomeretelomere fusion (t-t fusion) and regulating telomerase activity through a “protein-counting” system (31, 33, 34).”
BackgroundDesign, Synthesis, and Computational Studies of Inhibitors of Bcl-XL
Park, C., Oie, T., Petros, A. M., Zhang, H., Nimmer, P. M., Henry, R. F., & Elmore, S. W. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0650347 · Cited by 40
Kirkpatrick, D. T., Fan, Q., & Petes, T. D. (1999) · Genetics · doi:10.1093/genetics/152.1.101 · Cited by 40
Structural and Functional Studies of the Rap1 C-Terminus Reveal Novel Separation-of-Function Mutants
Feeser, E. A., & Wolberger, C. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.04.078 · Cited by 39
“Tethering the Rap1 C-terminus to DNA restores silencing in a Rap1 mutant strain(12) and causes a decrease in telomere length.(13) Yeast two-hybrid studies have demonstrated that the Rap1 C-terminal domain is sufficient for interactionwith the silencing proteins Sir3 and Sir4(14) as well as with the telomere length reg…”
BackgroundSua5p a single‐stranded telomeric DNA‐binding protein facilitates telomere replication
Meng, F., Hu, Y., Shen, N., Tong, X.-J., Wang, J., Ding, J., & Zhou, J. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.92 · Cited by 38
“Rif1 is an essential component of telomere length counting machinery (Marcand et al, 1997), whereas Pif1p inhibits telomerase activity through disassociating telomerase from telomeric DNA (Zhou et al, 2000; Boule et al, 2005).”
BackgroundSaccharomyces cerevisiae RAP1 binds to telomeric sequences with spatial flexibility
Wahlin, J. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.12.2292 · Cited by 39
Telomere maintenance and length regulation in Trypanosoma brucei
Horn, D., Spence, C., & Ingram, A. K. (2000) · The EMBO Journal · doi:10.1093/emboj/19.10.2332 · Cited by 40
The ins and outs of virulence gene expression: Mg2 as a regulatory signal
Groisman, E. A. (1998) · BioEssays · doi:10.1002/(sici)1521-1878(199801)20:1 · Cited by 100
Streamlined Method to Analyze 16S rRNA Gene Clone Libraries
Vergin, K. L., Rappé, M. S., & Giovannoni, S. J. (2001) · BioTechniques · doi:10.2144/01305bm03 · Cited by 38
Telomere-specific regulation of TERRA and its impact on telomere stability
Rivosecchi, J., Juríková, K., & Cusanelli, E. (2023) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2023.11.001 · Cited by 37
Fission yeast telomeres forecast the end of the crisis
Dehé, P.-M., & Cooper, J. P. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.07.045 · Cited by 45
“The Nakamura group confirmed the coupling between replication fork arrival at telomeres and telomerase recruitment [52,53].”
BackgroundFan, H., Chang, F.-W., Tsai, J., Lin, K., Chen, C., Lin, S., Liu, C.-A., & Harn, H. (2021) · Life · doi:10.3390/life11121405 · Cited by 39
“The shelterin complex and other protein complexes specific to the telomere can detect and react to c anges in telo ere length in order to maintain the proper length of telomeres [39,40] (Figure 1).”
BackgroundTelomere Dynamics in a Human Cancer Cell Line
Sprung, C. N., Sabatier, L., & Murnane, J. P. (1999) · Experimental Cell Research · doi:10.1006/excr.1998.4293 · Cited by 36
Investigating the role of the Est3 protein in yeast telomere replication
Lee, J., Mandell, E. K., Rao, T., Wuttke, D. S., & Lundblad, V. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkp1173 · Cited by 35
Telomeres: what's new at your end?
LeBel, C., & Wellinger, R. J. (2005) · Journal of Cell Science · doi:10.1242/jcs.02394 · Cited by 34
“Indeed, they somehow progressively inhibit telomeric repeat synthesis as the overall length of the particular telomere increases (Marcand et al., 1997; van Steensel and de Lange, 1997; Shore, 2001; Smogorzewska and de Lange, 2004).”
BackgroundThe yeast telomere length regulator TEL2 encodes a protein that binds to telomeric DNA
Kota, R. S., & Runge, K. W. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.6.1528 · Cited by 35
Stavenhagen, J. B., & Zakian, V. A. (1998) · Genes & Development · doi:10.1101/gad.12.19.3044 · Cited by 37
“RAP1 is important for TPE and telomere length control (see Kyrion et al. 1992, 1993; Marcand et al. 1997).”
BackgroundMatot, B., Bihan, Y. L., Lescasse, R., Pérez, J., Miron, S. M., David, G., Castaing, B., Weber, P., Raynal, B. D. E., Zinn‐Justin, S., et al. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr1166 · Cited by 34
Role of Pin2/TRF1 in telomere maintenance and cell cycle control
Zhou, X. Z., Perrem, K., & Lu, K. P. (2003) · Journal of Cellular Biochemistry · doi:10.1002/jcb.10496 · Cited by 34
“Furthermore, when the Rap1p carboxyl terminus is specifically targeted to an individual telomere, the number of repeats at the targeted telomere is reduced, which is proportional to the number of targeted molecules [Marcand et al., 1997].”
BackgroundInfluentialShepherding DNA ends: Rif1 protects telomeres and chromosome breaks
Fontana, G., Reinert, J. K., Thomä, N. H., & Rass, U. (2018) · Microbial Cell · doi:10.15698/mic2018.07.639 · Cited by 36
“The “protein counting” model postulates a negative feedback loop, by which the stochastic association of telomerase is increasingly suppressed when increasing amounts of Rap1, Rif1, and Rif2 are present [43, 47-51].”
Telomere biology of Trypanosomatids: more questions than answers
Cano, M. I. N. (2001) · Trends in Parasitology · doi:10.1016/s1471-4922(01)02014-1 · Cited by 33
At the end of the millennium, a view of the end
Shay, J. W. (1999) · Nature Genetics · doi:10.1038/70480 · Cited by 33
Telomeres and DNA damage checkpoints
Viscardi, V., Clerici, M., Cartagena‐Lirola, H., & Longhese, M. P. (2004) · Biochimie · doi:10.1016/j.biochi.2004.10.022 · Cited by 34
Kędziora, S., Gali, V. K., Wilson, R. H. C., Clark, K. R. M., Nieduszynski, C. A., Hiraga, S., & Donaldson, A. D. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky132 · Cited by 32
Sarig, G., Weisman-Shomer, P., & Fry, M. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7198 · Cited by 32
Dynamic Interactions of Arabidopsis TEN1: Stabilizing Telomeres in Response to Heat Stress
Lee, J. R., Xie, X., Yang, K., Zhang, J., Lee, S. Y., & Shippen, D. E. (2016) · The Plant Cell · doi:10.1105/tpc.16.00408 · Cited by 31
“Thisbinaryswitch iscontrolledby longrange protein interactions (Loayza and De Lange, 2003; Marcand et al., 1997), dynamic shifts among core components of telomere complexes (Jun et al., 2013), and posttranslational modification (Garg et al., 2014; Liu et al., 2014; Miyagawa et al., 2014; Zhang et…”
BackgroundTelomeres, senescence and cellular radiation response
Crompton, N. E. A. (1997) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050073 · Cited by 31
The telomerase cycle: normal and pathological aspects
Brunori, M., Luciano, P., Gilson, É., & G�li, V. (2005) · Journal of Molecular Medicine · doi:10.1007/s00109-004-0616-2 · Cited by 32
“The repressive chromatin complex, composed minimally of Rap1 and of two Rap1-interacting factors, Rif1 and Rif2, also involved in the Rap1-dependent regulation [76], was found to be dynamically remodeled over the course of the cell cycle [77].”
BackgroundInfluentialBeginning to Understand the End of the Chromosome
Cech, T. R. (2005) · Wiley eBooks · doi:10.1002/9783527620982.ch1 · Cited by 33
Xu, M., Kiselar, J., Whited, T. L., Hernandez-Sanchez, W. M., & Taylor, D. J. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1905381116 · Cited by 32
“In Saccharomyces cerevisiae, telomere length homeostasis is regulated by a protein-counting mechanism, whereby the length of the telomere DNA and the relative number of telomere proteins bound to it differentially influence telomerase-mediated extension (17, 18).”
BackgroundPOT1‐independent single‐strand telomeric DNA binding activities in Brassicaceae
Shakirov, E. V., McKnight, T. D., & Shippen, D. E. (2009) · The Plant Journal · doi:10.1111/j.1365-313x.2009.03837.x · Cited by 31
“, 1998), telomerase regulation (Marcand et al., 1997) and T-loop formation (Griffith et al.”
BackgroundKo, S., Jun, S., Bae, H., Byun, J.-S., Han, W., Park, H., Yang, S. W., Park, S., Jeon, Y. H., Cheong, C., et al. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn030 · Cited by 29
“Excess scRAP1 bound at the telomere negatively regulates telomere elongation in cis through the inhibition of telomerase activity (22,23).”
BackgroundRaymond, É., Soria, J., lzbicka, E., Boussin, F. D., Hurley, L. H., & Hoff, D. D. V. (2000) · Investigational New Drugs · doi:10.1023/a:1006373812586 · Cited by 31
“Basically, TRF1 regulates telomere length and TRF2 maintains telomere integrity [19, 32 ,33].”
BackgroundMte1 interacts with Mph1 and promotes crossover recombination and telomere maintenancePreprint
Silva, S. D. R., Altmannová, V., Luke-Glaser, S., Henriksen, P., Gallina, I., Yang, X., Choudhary, C., Luke, B., Krejčí, L., & Lisby, M. (2016) · Genes & Development · doi:10.1101/gad.276204.115 · Cited by 30
Characterization of the Yeast Telomere Nucleoprotein Core
Williams, T. L., Levy, D. L., Maki-Yonekura, S., Yonekura, K., & Blackburn, E. H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.170167 · Cited by 29
Saccharomyces cerevisiae Rif1 cooperates with MRX‐Sae2 in promoting DNA‐end resection
Martina, M., Bonetti, D., Villa, M., Lucchini, G., & Longhese, M. P. (2014) · EMBO Reports · doi:10.1002/embr.201338338 · Cited by 29
“Rif1 has been identified in Saccharomyces cerevisiae as a negative regulator of telomere length and transcriptional silencing [1,2].”
Quantitative Biology of Human Shelterin and Telomerase: Searching for the Weakest Point
Veverka, P., Janovič, T., & Hofr, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20133186 · Cited by 29
“Originally, the negative feedback loop for telomere length regulation was suggested in yeast by the Shore laboratory [62].”
BackgroundInhibition of yeast telomerase action by the telomeric ssDNA-binding protein, Cdc13p
Zappulla, D. C., Roberts, J. N., Goodrich, K. J., Cech, T. R., & Wuttke, D. S. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn830 · Cited by 28
“The observation that targeting the C-terminus of Rap1p to telomeres leads to telomere shortening, and that this is proportional to the number of molecules at a given telomere, led to the ‘protein-counting model’ of telomere length regulation by Rap1p (14).”
BackgroundDetection of Telomerase Activity in Tissues and Primary Cultured Lymphoid Cells of Penaeus japonicus
Lang, G.-H., Wang, Y., Nomura, N., & Matsumura, M. (2004) · Marine Biotechnology · doi:10.1007/s10126-003-0038-0 · Cited by 29
“In ciliated protozoa and yeast, telomerase is regulated and the average telomere length is maintained (Klobutcher et al., 1981; McEachern and Blackburn, 1995; Marcand et al., 1997).”
The C Terminus of the Major Yeast Telomere Binding Protein Rap1p Enhances Telomere Formation
Ray, A., & Runge, K. W. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.3.1284 · Cited by 30
“In addition, recent work has shown that yeast cells monitor the number of Rap1p C termini at each telomere (35, 42).”
BackgroundTelomerase in cancer: Clinical applications
Urquidi, V., Tarin, D., & Goodison, S. (1998) · Annals of Medicine · doi:10.3109/07853899809002483 · Cited by 29
The many types of heterogeneity in replicative senescence
Xu, Z., & Teixeira, M. T. (2019) · Yeast · doi:10.1002/yea.3433 · Cited by 29
Sudden Telomere Lengthening Triggers a Rad53-dependent Checkpoint inSaccharomyces cerevisiae
Viscardi, V., Baroni, E., Romano, M., Lucchini, G., & Longhese, M. P. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-11-0719 · Cited by 27
“It has been suggested that the Rap1/Rif complex may modulate telomerase activity by acting in a length-sensing mechanism based on the binding of one Rap1 protein per 15–18 base pairs of TG repeats (Conrad et al., 1990; Gilson et al., 1993; Marcand et al., 1997 ).”
BackgroundTelomere Length Regulation—A View from the Individual Chromosome Perspective
Slijepčević, P. (1998) · Experimental Cell Research · doi:10.1006/excr.1998.4185 · Cited by 28
At Short Telomeres Tel1 Directs Early Replication and Phosphorylates Rif1
Sridhar, A., Kędziora, S., & Donaldson, A. D. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004691 · Cited by 27
“Cells lacking either Rif1 or Rif2 have abnormally long telomeres due to uncontrolled lengthening by telomerase [13].”
BackgroundHwang, M. G., Kim, K., Lee, W.-K., & Cho, M. H. (2005) · Molecular Genetics and Genomics · doi:10.1007/s00438-004-1096-3 · Cited by 26
“…cerevisiae and Schizosaccharomyces pombe, respectively), and hTRF1 and hTRF2 from human are now well characterized (Chong et al. 1995; Cooper et al. 1997; Marcand et al. 1997; Smith et al. 1998; van Steensel et al. 1998; Kim et al. 1999; Li et al. 2000; Baumann and Cech 2001; Zhou and Lu 2001).”
BackgroundTelomeres and radiation-induced chromosome breakage
Shjepcevic, P., Natarajan, A. T., & Bryant, P. E. (1998) · Mutagenesis · doi:10.1093/mutage/13.1.45 · Cited by 27
TRF2 inhibition promotes anchorage-independent growth of telomerase-positive human fibroblasts
Brunori, M., Mathieu, N., Ricoul, M., Bauwens, S., Koering, C., de Climens, A. R., Belleville, A., Wang, Q., Puisieux, I., Décimo, D., et al. (2005) · Oncogene · doi:10.1038/sj.onc.1209135 · Cited by 26
“Telomeric proteins are essential to preserve chromosome stability by controlling telomere length, recombination and DNA damage checkpoint (Marcand et al., 1997; Ferreira and Cooper, 2001).”
BackgroundDynamics of Telomeric DNA Turnover in Yeast
McEachern, M. J., Underwood, D. H., & Blackburn, E. H. (2002) · Genetics · doi:10.1093/genetics/160.1.63 · Cited by 27
Metadata
- Authors
- Marcand, S., Gilson, E., & Shore, D.
- Affiliations
- École Normale Supérieure de Lyon (FR)
- E. Gilson, Laboratoire de Biologie Moléculaire et Cellulaire, Ecole Normale Supérieure de Lyon, UMR49 CNRS/ENSL, 69364 Lyon Cédex 07, France.
- University of Geneva (CH)
- Corresponding author
- Marcand, Stéphane
- Shore, David
- Venue
- Science
- Published
- 1997-02-14
- Volume
- 275
- Issue
- 5302
- Pages
- 986-990
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1978002329
- Cited by
- 524
- References
- 38
- Citations by year
- 2026: 10 · 2025: 4 · 2024: 7 · 2023: 6 · 2022: 5 · 2021: 14 · 2020: 5 · 2019: 17 · 2018: 10 · 2017: 12 · 2016: 13 · 2015: 9 · 2014: 14 · 2013: 14 · 2012: 10
- FWCI
- 23.60
- Type
- journal article
- Language
- en
- Open access
- Licence
- cc-by
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Funders
- National Institutes of Health (5r01gm040094-09)
- National Institute of General Medical Sciences (GM 40094)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Telomeres, Telomerase, and Senescence
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- telomere length regulation, Rap1p, feedback regulation, protein-DNA interactions, telomere elongation, Saccharomyces cerevisiae, telomere shortening
- MeSH terms
- Binding Sites, Fungal Proteins, Genetic Markers, Mutation, Saccharomyces cerevisiae, Transformation, Genetic, Chromosomes, Fungal, Gene Expression Regulation, Fungal, Telomere, Telomerase, GTP-Binding Proteins, rap GTP-Binding Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review