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In Vivo Effect of NusB and NusG on rRNA Transcription Antitermination
Open accessAbstract
Similarities between lambda and rRNA transcription antitermination have led to suggestions that they involve the same Nus factors. However, direct in vivo confirmation that rRNA antitermination requires all of the lambda Nus factors is lacking. We have therefore analyzed the in vivo role of NusB and NusG in rRNA transcription antitermination and have established that both are essential for it. We used a plasmid test system in which reporter gene mRNA was measured to monitor rRNA antiterminator-dependent bypass of a Rho-dependent terminator. A comparison of terminator read-through in a wild-type Escherichia coli strain and that in a nusB::IS10 mutant strain determined the requirement for NusB. In the absence of NusB, antiterminator-dependent terminator read-through was not detected, showing that NusB is necessary for rRNA transcription antitermination. The requirement for NusG was determined by comparing rRNA antiterminator-dependent terminator read-through in a strain overexpressing NusG with that in a strain depleted of NusG. In NusG-depleted cells, termination levels were unchanged in the presence or absence of the antiterminator, demonstrating that NusG, like NusB, is necessary for rRNA transcription antitermination. These results imply that NusB and NusG are likely to be part of an RNA-protein complex formed with RNA polymerase during transcription of the rRNA antiterminator sequences that is required for rRNA antiterminator-dependent terminator read-through.
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“Because Syn3A still has genes nusG/0840 and nusB/0107, both of which are factors required for rRNA transcription antitermination (Torres et al., 2004), we use an accelerated rate of 85 nt/s for transcription of the RNAP on the rRNA operons (Ryals et al., 1982).”
From Fundamental behaviors emerge from simulations of a living minimal cell (2022) · cites this paper as Torres et al., 2004
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Cites
Silhavy, T. J., Berman, M. L., & Enquist, L. W. (1984) · Medical Entomology and Zoology · Cited by 2,406
Maniatis, T. (1989) · Medical Entomology and Zoology · Cited by 1,171
Transcription termination and anti‐termination in E. coli
Nudler, E., & Gottesman, M. E. (2002) · Genes to Cells · doi:10.1046/j.1365-2443.2002.00563.x · Cited by 212
Transcription Processivity: Protein-DNA Interactions Holding Together the Elongation Complex
Nudler, E., Avetissova, E., Markovtsov, V. V., & Goldfarb, A. (1996) · Science · doi:10.1126/science.273.5272.211 · Cited by 194
Li, S. C., Squires, C. L., & Squires, C. L. (1984) · Cell · doi:10.1016/0092-8674(84)90280-0 · Cited by 182
Requirement for E. coli NusG protein in factor-dependent transcription termination
Sullivan, S. L., & Gottesman, M. E. (1992) · Cell · doi:10.1016/0092-8674(92)90041-a · Cited by 176
Jin, D. J., Burgess, R. R., Richardson, J. P., & Gross, C. A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.4.1453 · Cited by 175
CONTROL OF TRANSCRIPTION TERMINATION BY RNA-BINDING PROTEINS
Das, A. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.004333 · Cited by 147
Nodwell, J. R., & Greenblatt, J. (1993) · Cell · doi:10.1016/0092-8674(93)90665-d · Cited by 142
Ribosomal RNA operon anti-termination
Berg, K. L., Squires, C. L., & Squires, C. L. (1989) · Journal of Molecular Biology · doi:10.1016/0022-2836(89)90002-8 · Cited by 139
Research works printed but not linked: 1
- Bollag D. M. and S. J. Edelstein. 1991. Protein methods p. 181-211. Wiley-Liss Inc. New York N.Y.
Cited by
rRNA Transcription in Escherichia coli
Paul, B. J., Ross, W., Gaal, T., & Gourse, R. L. (2004) · Annual Review of Genetics · doi:10.1146/annurev.genet.38.072902.091347 · Cited by 336
“For example, the rRNA leader regions just upstream of the 16S and 23S rRNA genes contain boxA- and boxB-like sequences (13, 57), and the required protein factors for rRNA antitermination include NusA, NusB, NusE (r-protein S10), NusG, and r-protein S4 (61, 102, 103, 106, 107, 111).”
BackgroundNonaka, G., Blankschien, M. D., Herman, C., Gross, C. A., & Rhodius, V. A. (2006) · Genes & Development · doi:10.1101/gad.1428206 · Cited by 321
Mooney, R. A., Schweimer, K., ROSCH, P. J., Gottesman, M. E., & Landick, R. C. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.05.078 · Cited by 187
“These complexes are required for bacteriophage λ growth or for efficient transcription of ribosomal RNA operons.(6,7) This ability of NusG”
BackgroundStructural Basis for Transcript Elongation Control by NusG Family Universal Regulators
Kang, J. Y., Mooney, R. A., Nedialkov, Y. A., Saba, J., Mishanina, T. V., Artsimovitch, I., Landick, R. C., & Darst, S. A. (2018) · Cell · doi:10.1016/j.cell.2018.05.017 · Cited by 171
Fundamental behaviors emerge from simulations of a living minimal cell
Thornburg, Z. R., Bianchi, D. M., Brier, T. A., Gilbert, B. R., Earnest, E. E., Melo, M. C. R., Safronova, N., Sáenz, J. P., Cook, A. T., Wise, K. S., et al. (2022) · Cell · doi:10.1016/j.cell.2021.12.025 · Cited by 165
“Because Syn3A still has genes nusG/0840 and nusB/0107, both of which are factors required for rRNA transcription antitermination (Torres et al., 2004), we use an accelerated rate of 85 nt/s for transcription of the RNAP on the rRNA operons (Ryals et al.”
Spt4/5 stimulates transcription elongation through the RNA polymerase clamp coiled-coil motif
Hirtreiter, A., Damsma, G., Cheung, A., Klose, D., Grohmann, D., Vojnic, E., Martin, A. C. R., Cramer, P., & Werner, F. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq135 · Cited by 172
“Expression vectors for GST-fusion proteins of M. jannaschii Spt4/5, Spt5 NGN (1-82), Spt5 KOW (83–147) and Spt4 were generated by PCR amplification from genomic DNA and subcloning into BamHI (Spt5) and XhoI (Spt4) sites of pGEX-2TK (GE Healthcare).”
BackgroundMethodSigma and RNA Polymerase: An On-Again, Off-Again Relationship?
Mooney, R. A., Darst, S. A., & Landick, R. C. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.10.015 · Cited by 168
A Nexus for Gene Expression—Molecular Mechanisms of Spt5 and NusG in the Three Domains of Life
Werner, F. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.01.031 · Cited by 137
“NusG is a component of the antitermination complex that converts RNAP into a termination-resistant form, which is able to read through early intrinsic termination signals in, for example, ribosomal RNA (rrn) operons and during late gene expression of the bacteriophage lambda.(60) NusG stimulates processivity by suppre…”
BackgroundBacterial Transcription as a Target for Antibacterial Drug Development
Ma, C., Yang, X., & Lewis, P. J. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00055-15 · Cited by 130
“NusB and NusE are small transcription factors required for the formation of antitermination complexes that carry out rRNA synthesis (158, 188, 196).”
BackgroundHerbert, K. M., Zhou, J., Mooney, R. A., Porta, A. L., Landick, R. C., & Block, S. M. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.03.051 · Cited by 128
Bubunenko, M. G., Baker, T., & Court, D. L. (2007) · Journal of Bacteriology · doi:10.1128/jb.01713-06 · Cited by 114
“Since NusB is required for rRNA antitermination both in vitro (54) and in vivo ( 61 ), but not for cell growth, the Nus-dependent rRNA type of antitermination may not be an essential cellular process.”
BackgroundThe First Bite— Profiling the Predatosome in the Bacterial Pathogen Bdellovibrio
Lambert, C., Chang, C., Capeness, M. J., & Sockett, R. E. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008599 · Cited by 106
“in going from the non-replicative attack-phase to either HI or predatory conditions are, as would be expected, RNA polymerase genes including Bd2950, Bd2984 and rpoD sigma factor Bd0242; transcription factors and ribosomal genes and translation factors including anti-termination factors such as nusG Bd2992 [12] and gr…”
BackgroundLima, J., Auffret, M. D., Stewart, R. D., Dewhurst, R. J., Duthie, C.-A., Snelling, T. J., Walker, A. W., Freeman, T. C., Watson, M., & Roehe, R. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.00701 · Cited by 92
Deconstructing ribosome construction
Connolly, K., & Culver, G. M. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.01.011 · Cited by 90
Escherichia coli transcription factor NusG binds to 70S ribosomes
Saxena, S., Myka, K. K., Washburn, R. S., Costantino, N., Court, D. L., & Gottesman, M. E. (2018) · Molecular Microbiology · doi:10.1111/mmi.13953 · Cited by 76
“In conjunction with NusB, NusE (S10) and NusA, NusG promotes antitermination in rrn operons (Li et al., 1992; Zellars and Squires, 1999; Torres et al., 2004).”
Functional regions of the N‐terminal domain of the antiterminator RfaH
Belogurov, G. A., Sevostyanova, A., Svetlov, V. V., & Artsimovitch, I. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07056.x · Cited by 66
“Additionally, E. coli NusG cooperates with NusA, NusB, NusE and other factors to form specialized anti-termination complexes that are resistant to pause and termination signals (Zhou et al., 2002; Torres et al., 2004).”
BackgroundNusG-Spt5 Proteins—Universal Tools for Transcription Modification and Communication
Tomar, S. K., & Artsimovitch, I. (2013) · Chemical Reviews · doi:10.1021/cr400064k · Cited by 56
Regulation of Transcription Elongation and Termination
Washburn, R. S., & Gottesman, M. E. (2015) · Biomolecules · doi:10.3390/biom5021063 · Cited by 56
“The in vivo calculated/reported numbers for NusG [54] is one sixth the number of ribosomes ( 55,000 copies/cell, [55]).”
BackgroundViktorovskaya, O., Appling, F. D., & Schneider, D. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.202119 · Cited by 54
SuhB Associates with Nus Factors To Facilitate 30S Ribosome Biogenesis in Escherichia coli
Singh, N., Bubunenko, M. G., Smith, C., Abbott, D. M., Stringer, A. M., Shi, R., Court, D. L., & Wade, J. T. (2016) · mBio · doi:10.1128/mbio.00114-16 · Cited by 54
“Loop formation is mediated by SuhB, which likely bridges the gap between the elongating RNAP (bound to NusA and NusG), and the NusB/E-bound BoxA.”
BackgroundResultInfluentialYakhnin, A. V., FitzGerald, P. C., MCINTOSH, C. E., Yakhnin, H., Kireeva, M. L., Turek-Herman, J., Mandell, Z. F., Kashlev, M., & Babitzke, P. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2006873117 · Cited by 49
Bubunenko, M. G., Court, D. L., Refaii, A. A., Saxena, S., Korepanov, A. P., Friedman, D. I., Gottesman, M. E., & Alix, J. (2012) · Molecular Microbiology · doi:10.1111/mmi.12105 · Cited by 48
“…regions by the assembly of a transcription antitermination complex composed of at least the following proteins: NusA, NusB, NusG and NusE, as well as S4 and additional ribosomal proteins (Li et al., 1984; Sharrock et al., 1985; Squires et al., 1993; Torres et al., 2001; 2004; Quan et al., 2005).”
BackgroundInfluentialTranscriptional Polarity in rRNA Operons of Escherichia coli nusA and nusB Mutant Strains
Quan, S., Zhang, N., French, S. L., & Squires, C. L. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.5.1632-1638.2005 · Cited by 44
“In vivo studies have documented the importance of NusB and NusG for rRNA-AT and, in conjunction with BoxA, for increasing the rate of elongation by RNA polymerase (28, 32).”
BackgroundA multiplex CRISPR interference tool for virulence gene interrogation in Legionella pneumophila
Ellis, N. A., Kim, B., Tung, J., & Machner, M. P. (2021) · Communications Biology · doi:10.1038/s42003-021-01672-7 · Cited by 35
Replication Restart after Replication-Transcription Conflicts Requires RecA in Bacillus subtilis
Million‐Weaver, S., Samadpour, A. N., & Merrikh, H. (2015) · Journal of Bacteriology · doi:10.1128/jb.00237-15 · Cited by 37
“Antitermination factors such as NusB stabilize RNA polymerase in rRNA genes (64), and high expression from rRNA gene promoters maintains the DNA in these regions in a persistently underwound state behind the transcription apparatus, whereas positive supercoils accumulate ahead of RNAP.”
BackgroundIdentification of regulatory targets for the bacterial Nus factor complex
Baniulyte, G., Singh, N., Benoit, C. R., Johnson, R., Ferguson, R., Paramo, M. I., Stringer, A. M., Scott, A., Lapierre, P., & Wade, J. T. (2017) · Nature Communications · doi:10.1038/s41467-017-02124-9 · Cited by 37
Fnr (EtrA) acts as a fine-tuning regulator of anaerobic metabolism in Shewanella oneidensisMR-1
Cruz-García, C., Murray, A. E., Rodrigues, J. L. M., Gralnick, J. A., McCue, L. A., Romine, M. F., Löffler, F. E., & Tiedje, J. M. (2011) · BMC Microbiology · doi:10.1186/1471-2180-11-64 · Cited by 35
“coli was also shown [41,42].”
Burmann, B. M., Scheckenhofer, U., Schweimer, K., & ROSCH, P. J. (2011) · Biochemical Journal · doi:10.1042/bj20101679 · Cited by 34
Evolutionary Comparison of Ribosomal Operon Antitermination Function
Arnvig, K. B., Zeng, S. H., Quan, S., Papageorge, A. T., Zhang, N., Villapakkam, A. C., & Squires, C. L. (2008) · Journal of Bacteriology · doi:10.1128/jb.00760-08 · Cited by 32
“Antitermination requires the association of proteins NusA, NusB, and NusG, as well as ribosomal proteins, with the transcription elongation complex (28, 37, 46, 47).”
BackgroundCagliero, C., Zhou, Y. N., & Jin, D. J. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1103 · Cited by 30
Wenzel, S., Martins, B. M., ROSCH, P. J., & Wöhrl, B. M. (2009) · Biochemical Journal · doi:10.1042/bj20091422 · Cited by 29
The dynamic nature and territory of transcriptional machinery in the bacterial chromosome
Cagliero, C. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00497 · Cited by 31
“NusB is thought to bind in vivo to the BoxA RNA sequences of nascent rRNAmolecules and is also involved in rRNA processing (Torres et al., 2004; Bubunenko et al., 2013).”
BackgroundA high-affinity interaction between NusA and the rrn nut site in Mycobacterium tuberculosis
Arnvig, K. B., Pennell, S., Gopal, B., & Colston, M. J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401287101 · Cited by 29
Burmann, B. M., Luo, X., ROSCH, P. J., Wahl, M. C., & Gottesman, M. E. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp736 · Cited by 27
“In the case of nut, N protein forms part of the complex, whereas the complex that forms at rrn nut includes the Nus proteins and a number of additional host factors (21,22).”
BackgroundTranscription termination and antitermination of bacterial CRISPR arrays
Stringer, A. M., Baniulyte, G., Lasek‐Nesselquist, E., Seed, K. D., & Wade, J. T. (2020) · eLife · doi:10.7554/elife.58182 · Cited by 25
“The Nus complex prevents Rho termination (10, 11) in a BoxA-dependent manner (11–13), and BoxA elements are found in phylogenetically diverse copies of rRNA (14, 15).”
BackgroundSubcellular Partitioning of Transcription Factors inBacillus subtilis
Doherty, G. P., Meredith, D. H., & Lewis, P. J. (2006) · Journal of Bacteriology · doi:10.1128/jb.01934-05 · Cited by 26
Sayyed, H. E., Pambos, O. J., Stracy, M., Gottesman, M. E., & Kapanidis, A. N. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.01.025 · Cited by 26
Ye, J., Yang, X., & Ma, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010339 · Cited by 25
Ancient Transcription Factors in the News
Artsimovitch, I., & Knauer, S. H. (2019) · mBio · doi:10.1128/mbio.01547-18 · Cited by 27
“However, a recent medium-resolution cryo-EM structure of a complete N-dependent TAC ( N-TAC) that contains NusA, NusB, NusE, and NusG and N paints a picture in which protein-protein contacts take center stage instead (46).”
BackgroundInfluentialQiu, Y., Chan, S. T., Lin, L., Shek, T. L., Tsang, T. F., Zhang, Y., Ip, M., Chan, P. K. S., Blanchard, N., Hanquet, G., et al. (2019) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2019.103203 · Cited by 24
Transcription elongation: Heterogeneous tracking of RNA polymerase and its biological implications
Imashimizu, M., Shimamoto, N., Oshima, T., & Kashlev, M. (2014) · Transcription · doi:10.4161/trns.28285 · Cited by 25
“Bacterial NusG increases the elongation rate by inhibiting backtracking,(23,24) which, for example, is critical for uninterrupted and rapid elongation of rRNA.(25) Archaea and eukaryotes have Spt5, the counterpart of NusG.”
BackgroundTselykh, T. V., Roos, C., & Heino, T. I. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.03.037 · Cited by 22
“The KOW-motif-containing proteins have been shown to play a role in transcriptional anti-termination and in the regulation of translation [44–47].”
BackgroundSuhB is an integral part of the ribosomal antitermination complex and interacts with NusA
Dudenhoeffer, B. R., Schneider, H., Schweimer, K., & Knauer, S. H. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz442 · Cited by 21
“Despite some functional similarities of N-dependent and rrn AT (38,57), no central unstructured component such as N has yet been identified in rrn AT.”
BackgroundGrohmann, D., & Werner, F. (2010) · RNA Biology · doi:10.4161/rna.7.3.11912 · Cited by 20
Marchi, P., Longhi, V., Zangrossi, S., Gaetani, E., Briani, F., & Dehò, G. (2007) · Molecular Genetics and Genomics · doi:10.1007/s00438-007-0231-3 · Cited by 19
“RNA polymerase travelling through such a long untranslated region is insured by the assembly of a highly processive, Rho-insensitive transcription elongation complex, which includes NusA, NusB, NusE, and NusG factors, at speciWc “nut-like” sequences in the rRNA operon leader region (reviewed by Condon et al. 1995; Tor…”
BackgroundYu, P., Zhao, Y., Jiang, Y., Yang, Y., Liu, X., Zhang, H., Zhao, J., Lee, Y. K., Zhang, H., & Chen, W. (2021) · Food Bioscience · doi:10.1016/j.fbio.2021.101381 · Cited by 18
Martín, C. M., Sun, Z., Zhou, Y. N., & Jin, D. J. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.01115 · Cited by 16
“The 3D images of multicolor superresolution Structured Illumination Microscopy (3D-SIM) reveal that under optimal growth conditions (LB at 37C), RNAP foci, spatially located at the periphery of the compact nucleoid, co-localize with transcriptional factors, NusA and NusB, both of which are involved in rRNA synthesis a…”
BackgroundWang, C., Long, X., Mao, X., Dong, H., Xu, L., & Li, Y. (2009) · Microbiological Research · doi:10.1016/j.micres.2009.05.003 · Cited by 18
“coli (Torres et al., 2004), which could affect the transcriptional elongation rate, and was necessary for the proper folding of rRNA and the subsequent assembly of ribosomal subunit (Vogel and Jensen 1997; Zhou et al.”
BackgroundAn Autoinhibited State in the Structure of Thermotoga maritima NusG
Drögemüller, J., Stegmann, C. M., Mandal, A., Steiner, T., Burmann, B. M., Gottesman, M. E., Wöhrl, B. M., ROSCH, P. J., Wahl, M. C., & Schweimer, K. (2013) · Structure · doi:10.1016/j.str.2012.12.015 · Cited by 17
“…an additional domain (domain II) is inserted in the NTD (Figure S1 available online) (Knowlton et al., 2003; Liao et al., 1996; Steiner et al., 2002) and a similar domain expansion is found in the functional NusG analog, Spt5, of archaea and eukaryotes (Guo et al., 2008; Wenzel et al., 2010).”
BackgroundControl of Ribosome Synthesis During the Cell Division Cycles ofE. coliandSynechococcus
Asato, Y. (2005) · Current Issues in Molecular Biology · doi:10.21775/cimb.007.109 · Cited by 17
“The antitermination complexes, composed of r-proteins S10 (=NusE), S4, L3, L4 L13 and Nus factors (A, B, G) are able to permit read-through of nut sites (Torres et al., 2001; Luttgen et al., 2002;Torres et al., 2004).”
BackgroundLewis, P. J., Doherty, G. P., & Clarke, J. (2008) · Microbiology · doi:10.1099/mic.0.2008/018549-0 · Cited by 14
“coli and Mycobacterium tuberculosis suggesting that it is restricted to antitermination complex formation (Torres et al., 2004; Greive et al., 2005).”
BackgroundResultRichardson, L. V., & Richardson, J. P. (2005) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2005.04.002 · Cited by 14
RNA Polymerase's Relationship with the Ribosome: Not So Physical, Most of the Time
Chen, M., & Fredrick, K. L. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.03.018 · Cited by 12
Guo, G., Gao, Y., Zhu, Z., Zhao, D., Liu, Z., Zhou, H., Niu, L., & Teng, M. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.09.023 · Cited by 11
“In bacteria, NusG suppresses pausing and increases elongation rate (Burova and Gottesman, 1995; Torres et al., 2004), and is also necessary for rho-dependent transcription termination (Cardinale et al.”
BackgroundReplication initiator DnaA interacts with an anti-terminator NusG in T. tengcongensis
Liu, J., Pei, H., Mei, S., Li, J., Zhou, L., & Xiang, H. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.04.131 · Cited by 11
“anti-terminator, it accelerates the rate of RNA chain growth by RNA polymerase (RNAP) [14], and makes RNA polymerase readthrough transcription terminators in rrn operons [15,16].”
Thermotoga maritimaNusG: domain interaction mediates autoinhibition and thermostability
Drögemüller, J., Schneider, C., Schweimer, K., Strauß, M., Wöhrl, B. M., ROSCH, P. J., & Knauer, S. H. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1111 · Cited by 9
Vassylyeva, M. N., Svetlov, V. V., Klyuyev, S., Devedjiev, Y. D., Artsimovitch, I., & Vassylyev, D. G. (2006) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s174430910603658x · Cited by 9
“Antitermination of transcription is typically mediated by multi-protein assemblies (Torres et al., 2004; Weisberg & Gottesman, 1999); in contrast, RfaH increased the rate of transcription in the absence of other regulatory proteins (Artsimovitch & Landick, 2002).”
BackgroundZheng, Y., Kan, C. H., Tsang, T. F., Liu, Y., Liu, T., Tsang, M. W., Lam, L. Y., Yang, X., & Ma, C. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01386 · Cited by 6
Jin, D. J., Cagliero, C., Izard, J., Martín, C. M., & Zhou, Y. N. (2016) · Wiley eBooks · doi:10.1002/9781119004813.ch6 · Cited by 3
Fleurier, S., & Matić, I. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1034 · Cited by 2
“In E. coli , the BoxA rRNA sequence serves as a nucleation site for the formation of the Nus-factor-dependent antitermination complex, which prevents Rho-dependent termination, reduces RNAP pausing, and increases transcription elongation rates [ 57 ].”
Segev, E., Pasternak, Z., Sasson, T. B., Jurkevitch, É., & Gonen, M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0195537 · Cited by 1
Transcription Termination and Antitermination of Bacterial CRISPR ArraysPreprint
Stringer, A. M., Baniulyte, G., Lasek‐Nesselquist, E., Seed, K. D., & Wade, J. T. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/405316 · Cited by 1
Accessory factors for ribosomal assembly
Lövgren, M. (2004) · DiVA at Umeå University (Umeå University)
Luo, X. (2010) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3304
Mechanism of Transcription Arrest By The Nun Protein of Bacteriophage HK022
Vitiello, C. L. (2012) · doi:10.7916/d85t3sk4
Regulation of transcription elongation and termination
(1991) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240471106
Sayyed, H. E., Pambos, O. J., Stracy, M., Gottesman, M. E., & Kapanidis, A. N. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.21.517430
“Processive anti-termination is mediated by a complex of proteins interacting with RNAP to counteract premature termination 7,33 and ensure efficient rrn operon transcription.”
Weiler, J., Lapp, C. J., Gescher, J., & Edel, M. (2026) · SSRN Electronic Journal · doi:10.2139/ssrn.7071668
Metadata
- Authors
- Torres, M., Balada, J.-M., Zellars, M., Squires, C., & Squires, C. L.
- Affiliations
- King Faisal Specialist Hospital & Research Centre (SA)
- Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111
- Tufts University (US)
- Corresponding author
- Squires, Craig
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 2004-03
- Volume
- 186
- Issue
- 5
- Pages
- 1304-1310
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC344418
- OpenAlex
- W2164650717
- Cited by
- 68
- References
- 40
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 2 · 2022: 3 · 2021: 2 · 2020: 3 · 2019: 4 · 2018: 5 · 2017: 1 · 2016: 4 · 2015: 4 · 2014: 2 · 2013: 2 · 2012: 3
- FWCI
- 2.32
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Bacteriology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM024751, GM24751)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- NusB, NusG, rRNA transcription, antitermination, Rho-dependent transcription termination, RNA polymerase, protein-RNA complex, Escherichia coli
- MeSH terms
- Escherichia coli, Mutation, Peptide Elongation Factors, Rho Factor, RNA, Messenger, RNA, Ribosomal, Terminator Regions, Genetic, Transcription Factors, Transcription, Genetic, Blotting, Western, Gene Expression Regulation, Bacterial, Escherichia coli 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 ›
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
