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Xer-mediated site-specific recombination in vitro
Open accessAbstract
The Xer site-specific recombination system acts at ColE1 cer and pSC101 psi sites to ensure that these plasmids are in a monomeric state prior to cell division. We show that four proteins, ArgR, PepA, XerC and XerD are necessary and sufficient for recombination between directly repeated cer sites on a supercoiled plasmid in vitro. Only PepA, XerC and XerD are required for recombination at psi in vitro. Recombination at cer and psi in vitro requires negative supercoiling and is exclusively intramolecular. Strand exchange at cer produces Holliday junction-containing products in which only the top strands have been exchanged. This reaction requires the catalytic tyrosine residue of Xer C but not that of XerD. Recombination at psi gives catenated circular resolution products. Strand exchange at psi is sequential. XerC catalyses the first (top) strand exchange to make a Holiday junction intermediate and XerD catalyses the second (bottom) strand exchange.
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“The 11-kb LIR encoded a tyrosine recombinase that belonged to the integrase family.43 , 44”
From Whole genomic DNA sequencing and comparative genomic analysis of Arthrospira platensis: high genome plasticity and genetic diversity (2016) · cites this paper as [44]
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Self-citationCrystal structure of the site‐specific recombinase, XerD
Subramanya, H. S., Arciszewska, L. K., Baker, R. A., Bird, L. E., Sherratt, D. J., & Wigley, D. B. (1997) · The EMBO Journal · doi:10.1093/emboj/16.17.5178 · Cited by 210
Self-citationSarnovsky, R. J., May, E. W., & Craig, N. L. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01024.x · Cited by 160
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BackgroundVal, M., Bouvier, M., Campos, J., Sherratt, D. J., Cornet, F., Mazel, D., & Barre, F. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.07.002 · Cited by 153
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BackgroundSelf-citationTiming, self‐control and a sense of direction are the secrets of multicopy plasmid stability
Summers, D. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.01012.x · Cited by 138
“, 1989) are required to mediate site-specific recombination in vivo and in vitro (Colloms et al., 1996).”
BackgroundInfluentialSträter, N., Sherratt, D. J., & Colloms, S. D. (1999) · The EMBO Journal · doi:10.1093/emboj/18.16.4513 · Cited by 131
“The arginine repressor (ArgR) and aminopeptidase A (PepA) are accessory proteins which are not directly involved in the strand exchange reaction but are absolutely required for recombination at cer in vivo and in vitro (Stirling et al., 1988, 1989; Colloms et al., 1996).”
BackgroundSelf-citationSunnerhagen, M., Nilges, M., Otting, G., & Carey, J. (1997) · Nature Structural Biology · doi:10.1038/nsb1097-819 · Cited by 118
Topological Selectivity in Xer Site-Specific Recombination
Colloms, S. D., Bath, J., & Sherratt, D. J. (1997) · Cell · doi:10.1016/s0092-8674(00)81931-5 · Cited by 115
Self-citationFtsK‐dependent and ‐independent pathways of Xer site‐specific recombination
Recchia, G. D., Aroyo, M., Wolf, D., Blakely, G., & Sherratt, D. J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.20.5724 · Cited by 113
“Conversion of a plasmid containing two directly repeated dif sites (pSDC124) to a derivative containing a single dif site is dependent on the presence of XerC and XerD, and can occur by either intramolecular recombination or a combination of inter- and intramolecular recombination.”
BackgroundInfluentialSelf-citationBarre, F., Aroyo, M., Colloms, S. D., Helfrich, A., Cornet, F., & Sherratt, D. J. (2000) · Genes & Development · doi:10.1101/gad.188700 · Cited by 110
“However, in the absence of EtBr, XerCD appeared to generate no recombinant product and little or no HJs when they were reacted with a supercoiled molecule containing two dif sites (Colloms et al. 1996).”
BackgroundMethodResultSelf-citationCollis, C. M., Kim, M., Stokes, H. W., & Hall, R. M. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00936.x · Cited by 111
“However, other integrases with the same Y → F substitution have also been found to retain residual in vitro strand cleavage activity (Han et al., 1993) or in vivo recombination ability (Blakely et al., 1993; Colloms et al., 1996).”
BackgroundInfluentialBiosynthesis of Arginine and Polyamines
Charlier, D., & Glansdorff, N. (2004) · EcoSal Plus · doi:10.1128/ecosalplus.3.6.1.10 · Cited by 106
Polynucleotidyl transfer reactions in site‐specific DNA recombination
Mizuuchi, K. (1997) · Genes to Cells · doi:10.1046/j.1365-2443.1997.970297.x · Cited by 100
“1989), Xer recombination with certain substrates (Blakely & Sherratt 1996; Colloms et al. 1996), and transposition reactions such as Mu (Craigie & Mizuuchi 1986).”
BackgroundModulation of ColE1-Like Plasmid Replication for Recombinant Gene Expression
Camps, M. (2010) · Recent Patents on DNA & Gene Sequences · doi:10.2174/187221510790410822 · Cited by 98
“ColE1-like plasmids encode a 250bp region (the cer site [24]) that resolves multimers through site-specific recombination mediated by host proteins [25].”
BackgroundNew Insight into Site-Specific Recombination from Flp Recombinase-DNA Structures
Chen, Y., & Rice, P. A. (2003) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.32.110601.141732 · Cited by 97
λ Integrase and the λ Int Family
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Steiner, W. W., & Kuempel, P. L. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00651.x · Cited by 90
Decatenation of DNA circles by FtsK‐dependent Xer site‐specific recombination
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Self-citationChallenging a Paradigm: the Role of DNA Homology in Tyrosine Recombinase Reactions
Rajeev, L., Malanowska, K., & Gardner, J. F. (2009) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00038-08 · Cited by 87
“This was expected since only a single top-strand exchange mediated by XerC occurs at cer (20).”
BackgroundXer Site Specific Recombination: Double and Single Recombinase Systems
Martinez, F. A. C., Benmohamed, A., & Szatmari, G. B. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.00453 · Cited by 87
Reciprocal Control of Catalysis by the Tyrosine Recombinases XerC and XerD
Hallet, B., Arciszewska, L. K., & Sherratt, D. J. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80224-5 · Cited by 84
Self-citationMidonet, C., & Barre, F. (2014) · Microbiology Spectrum · doi:10.1128/microbiolspec.mdna3-0056-2014 · Cited by 74
Plasmid Diversity and Adaptation Analyzed by Massive Sequencing of Escherichia coli Plasmids
de Toro, M., Garcillán-Barcia, M. P., & de la Cruz, F. (2014) · Microbiology Spectrum · doi:10.1128/microbiolspec.plas-0031-2014 · Cited by 71
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Identification and Characterization of the dif Site from Bacillus subtilis
Sciochetti, S. A., Piggot, P. J., & Blakely, G. W. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.3.1058-1068.2001 · Cited by 64
“By convention, the top strand is the first XerC-mediated strand exchange during site-specific recombination at the psi site (13).”
The isomeric preference of Holliday junctions influences resolution bias by λ integrase
Azaro, M. A., & Landy, A. (1997) · The EMBO Journal · doi:10.1093/emboj/16.12.3744 · Cited by 64
Dissection of a functional interaction between the DNA translocase, FtsK, and the XerD recombinase
Yates, J. R., Zhekov, I., Baker, R., Eklund, B., Sherratt, D. J., & Arciszewska, L. K. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.05033.x · Cited by 63
“…four amino acids are specifically involved in the interactions with FtsKC, their substitution should not affect the ability of Ec XerD to mediate recombination of DNA substrates that do not require activation by Ec FtsKC, for example, the plasmid recombination site, psi (Colloms et al., 1996).”
BackgroundSelf-citationCheng, Y., Chen, Y., Liu, Y., Guo, Y., Zhou, Y., Xiao, T., Zhang, S., Xu, H., Chen, Y., Shan, T., et al. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1803769 · Cited by 62
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BackgroundCharacterization of XerC‐ and XerD‐dependent CTX phage integration in Vibrio cholerae
McLeod, S. M., & Waldor, M. K. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04309.x · Cited by 60
“…processing enzyme, RuvC, can resolve Holliday structures formed by E. coli XerC and XerD in vitro at cer sites; moreover, RuvC preferentially cleaves the non-recombinant strands of this structure resulting in recombinant rather than parental products (McCulloch et al., 1994; Colloms et al., 1996).”
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“In vitro recombination was carried out essentially as described previously (Colloms et al., 1996), using approximately 300 ng of pSDC134 in 20 ml of a buffer containing 50 mM Tris-HCl, pH 8.0, 50 mM NaCl, 5 mM spermidine (HCl)3, 1.25 mM EDTA and 25 mg ml ¹1 BSA.”
BackgroundMethodInfluentialSelf-citationFtsK DNA Translocase: The Fast Motor That Knows Where It's Going
Crozat, E., & Grainge, I. (2010) · ChemBioChem · doi:10.1002/cbic.201000347 · Cited by 58
Blakely, G. W., Davidson, A. O., & Sherratt, D. J. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0709 · Cited by 58
Self-citationPérals, K., Capiaux, H., Vincourt, J., Louarn, J., Sherratt, D. J., & Cornet, F. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02277.x · Cited by 57
“Recombination between natural plasmid-borne Xer sites requires additional sequences and proteins, whose role is to ensure that recombination is preferentially intramolecular, converting plasmid multimers to monomers (Summers, 1989; Blakely and Sherratt, 1996; Colloms et al., 1996; AleÂn et al., 1997).”
BackgroundSelf-citationDNA excision by the SfiI restriction endonuclease
Nobbs, T. J., Szczelkun, M. D., Wentzell, L. M., & Halford, S. E. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1966 · Cited by 57
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“In Results we show that, for Xer recombination, all tangle solutions in the parallel sites case correspond to RZ(G1) as predicted by the HJ.”
BackgroundMethodInfluentialSelf-citationAction of site‐specific recombinases XerC and XerD on tethered Holliday junctions
Arciszewska, L. K., Grainge, I., & Sherratt, D. J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.12.3731 · Cited by 55
Self-citationSpecies specificity in the activation of Xer recombination at dif by FtsK
Yates, J. R., Aroyo, M., Sherratt, D. J., & Barre, F. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03574.x · Cited by 54
“© 2003 Blackwell Publishing Ltd, Molecular Microbiology, 49, 241–249 Protein purification Escherichia coli XerC, XerD and FtsK were purified as described previously (Colloms et al., 1996; Aussel et al., 2002).”
MethodSelf-citationMartin, S. S., Pulido, E., Chu, V. C., Lechner, T. S., & Baldwin, E. P. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00246-2 · Cited by 53
“The elegance of this mechanism is in contrast to XerCD/dif-mediated chromosome segregation, in which strand exchange order and site alignment are assured by two distinct recombinase proteins that interact specifically with their unique half-sites.(51)”
Hojgaard, A., Szerlong, H. J., Tabor, C., & Kuempel, P. L. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01545.x · Cited by 52
“Maintenance of negative supercoiling would be very important for continued replication and transcription in this region and, later on, it would also be required for XerC/XerD-mediated recombination at dif (Colloms et al., 1996).”
BackgroundGlew, M. D., Marenda, M. S., Rosengarten, R., & Citti, C. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.21.5987-5998.2002 · Cited by 51
“The Xer site-specific recombination system has been best studied in Escherichia coli and consists of two homologous recombinases, XerC and XerD, which act on specific chromosomal sequences called dif sites to initiate DNA strand exchange to resolve chromosome dimers that have arisen from homologous recombination befor…”
BackgroundSciochetti, S. A., Piggot, P. J., Sherratt, D. J., & Blakely, G. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.19.6053-6062.1999 · Cited by 50
“When XerC and XerD are incubated with the dif-HJ substrate, the major product is derived from an XerC-mediated exchange of top strands (by convention, the first strand exchanged in recombination at psi) (7).”
BackgroundSelf-citationMutagenesis of PepA suggests a new model for the Xer/cer synaptic complex
Reijns, M. A. M., Lu, Y., Leach, S., & Colloms, S. D. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04716.x · Cited by 50
Self-citationMulticopy plasmid stability: Revisiting the dimer catastrophe
Field, C. M., & Summers, D. (2011) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2011.09.006 · Cited by 49
Xer Site‐Specific Recombination: Promoting Chromosome Segregation
Barre, F., & Sherratt, D. J. (2007) · doi:10.1128/9781555817954.ch8 · Cited by 49
Self-citationArciszewska, L. K., Baker, R. A., Hallet, B., & Sherratt, D. J. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3762 · Cited by 46
Self-citationDeterminants of selectivity in Xer site-specific recombination.Preprint
Blakely, G., & Sherratt, D. J. (1996) · Genes & Development · doi:10.1101/gad.10.6.762 · Cited by 45
“We believe that this resolution selectivity results from the use of a "topological filter" that ensures that productive synaptic complexes, which must have a fixed protein/DNA geometry, can only form and recombine on supercoiled substrates containing two directly repeated recombination sites (discussed in Boocock et a…”
BackgroundSelf-citationXer Recombination in Escherichia coli
Cornet, F., Hallet, B., & Sherratt, D. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.21927 · Cited by 44
Self-citationAccessory factors determine the order of strand exchange in Xer recombination at psi
Bregu, M., Sherratt, D. J., & Colloms, S. D. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf379 · Cited by 44
Self-citationSequential Strand Exchange by XerC and XerD during Site-specific Recombination at dif
Blakely, G. W., Davidson, A. O., & Sherratt, D. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.14.9930 · Cited by 44
Self-citationGenetic Mechanisms of Surface Variation
Yogev, D., Browning, G. F., & Wise, K. S. (2002) · Springer eBooks · doi:10.1007/0-306-47606-1_19 · Cited by 43
Sequence of the loxP Site Determines the Order of Strand Exchange by the Cre Recombinase
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“Indeed supercoiling appears to be a supplementary requirement for efficient dimer resolution (13).”
BackgroundMethodAre two better than one? Analysis of an FtsK/Xer recombination system that uses a single recombinase
Nolivos, S., Pages, C., Rousseau, P., Bourgeois, P., & Cornet, F. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq507 · Cited by 40
“This ‘‘XerC-first’’ pattern applies to activities of XerCD other than the resolution of chromosome dimers: during the resolution of plasmid multimers at the psi or cer sites (8) and during the integration of bacteriophage genomes into their host dif sites (9).”
BackgroundXu, T., Qin, S., Hu, Y., Song, Z., Ying, J., Li, P., Dong, W., Zhao, F., Yang, H., & Bao, Q. (2016) · DNA Research · doi:10.1093/dnares/dsw023 · Cited by 37
“The 11-kb LIR encoded a tyrosine recombinase that belonged to the integrase family.(43,44) After a sequence replication event, fusion of the 11-kb copy into adjacent loci of genome might have resulted from the integrasemediated site-specific recombination, which well explains the duplication events.”
BackgroundThe Quiescent-Cell Expression System for Protein Synthesis in Escherichia coli
Rowe, D., & Summers, D. (1999) · Applied and Environmental Microbiology · doi:10.1128/aem.65.6.2710-2715.1999 · Cited by 39
“Dimers and higher multimers of ColE1 and other natural plasmids are resolved to monomers by unidirectional, sitespecific recombination requiring a 250-bp region of ColE1 (the cer site [28]) and at least four proteins (XerC, XerD, ArgR, and PepA) encoded by the host bacterium (5).”
BackgroundTolmasky, M. E., Colloms, S. D., Blakely, G., & Sherratt, D. J. (2000) · Microbiology · doi:10.1099/00221287-146-3-581 · Cited by 38
“This cer-like region contains a recombination core with good matches to consensus XerC- and XerD-binding sites (Blakely et al., 1993; Colloms et al., 1996).”
BackgroundMethodInfluentialSelf-citationBalalovski, P., & Grainge, I. (2020) · Molecular Microbiology · doi:10.1111/mmi.14563 · Cited by 38
“In the recombination reactions at both cer and psi the initial cleavage and strand transfer that produces a Holliday junction is mediated by XerC (Colloms et al., 1996).”
BackgroundDery, K. J., Chavideh, R., Waters, V. L., Chamorro, R., Tolmasky, L. S., & Tolmasky, M. E. (1997) · Plasmid · doi:10.1006/plas.1997.1303 · Cited by 38
Hayes, F., & Sherratt, D. J. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0828 · Cited by 38
Self-citationThe topology of plasmid-monomerizing Xer site-specific recombination
Colloms, S. D. (2013) · Biochemical Society Transactions · doi:10.1042/bst20120340 · Cited by 37
Self-citationNucleoprotein architecture and ColE1 dimer resolution: a hypothesis
Hodgman, C. T., Griffiths, H., & Summers, D. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00948.x · Cited by 36
“However, recombination in vitro becomes ArgR independent in the presence of an abnormally high PepA concentration (Colloms et al., 1996).”
BackgroundInfluentialSense and nonsense from a systems biology approach to microbial recombinant protein production
Sevastsyanovich, Y. R., Alfasi, S., & Cole, J. A. (2010) · Biotechnology and Applied Biochemistry · doi:10.1042/ba20090174 · Cited by 35
Control of Cre recombination by regulatory elements from Xer recombination systems
Gourlay, S. C., & Colloms, S. D. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2003.03962.x · Cited by 32
“Consistent with this, recombination in vitro at cer requires ArgR at low concentration of PepA but can occur in the absence of ArgR at high PepA concentrations (Colloms et al., 1996).”
BackgroundMethodInfluentialSelf-citationDirectional Resolution of Synthetic Holliday Structures by the Cre Recombinase
Lee, L. S., & Sadowski, P. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103739200 · Cited by 32
Cao, Y., Hallet, B., Sherratt, D. J., & Hayes, F. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1380 · Cited by 31
Self-citationCharacterization of a conjugative transposon integrase, IntDOT
Malanowska, K., Salyers, A. A., & Gardner, J. F. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05164.x · Cited by 30
“The XerD (Y279F) mutation has no effect on the reaction at cer in vitro; in contrast, it is inactive when used in a psi recombination reaction. g.”
BackgroundInfluentialTopology of Xer Recombination on Catenanes Produced by Lambda Integrase
Bath, J., Sherratt, D. J., & Colloms, S. D. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2804 · Cited by 30
Self-citationDNA binding of Escherichia coli arginine repressor mutants altered in oligomeric state
Chen, S., Merican, A. F., & Sherratt, D. J. (1997) · Molecular Microbiology · doi:10.1046/j.1365-2958.1997.4301791.x · Cited by 30
“Both ArgR and PepA appear to act as architectural proteins around which two distant segments of DNA are interwound with a precise geometry (Colloms et al., 1996; 1997; Alén et al., 1997).”
BackgroundResultInfluentialSelf-citationSite‐specific recombination at dif by Haemophilus influenzae XerC
Neilson, L., Blakely, G., & Sherratt, D. J. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01231.x · Cited by 30
“EcoXerDY279F was purified according to Colloms et al. (1996).”
BackgroundInfluentialSelf-citationSong, H., Wang, H., Gigot, D., Dimova, D., Sakanyan, V. A., Glansdorff, N., & Charlier, D. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5236 · Cited by 26
Lin, D. L., Traglia, G. M., Baker, R., Sherratt, D. J., Ramirez, M. S., & Tolmasky, M. E. (2020) · Antibiotics · doi:10.3390/antibiotics9070405 · Cited by 25
“In other cases, like the ColE1 plasmid cer [39] or the pJHCMW1 plasmid mwr [40], XerD is needed to activate XerC, which catalyzes the formation of the Holliday junction, which is then processed independently of XerD, most probably by DNA replication [9,10,41,42].”
BackgroundSelf-citationZerbib, D., Colloms, S. D., Sherratt, D. J., & West, S. C. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1157 · Cited by 25
Self-citationC‐terminal interactions between the XerC and XerD site‐specific recombinases
Spiers, A. J., & Sherratt, D. J. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01418.x · Cited by 24
“Complete recombination reactions on supercoiled psi-containing plasmid substrates can be assayed in vitro (Colloms et al., 1996; 1997), whereas a whole variety of recombination sites can be assayed in vivo (Summers and Sherratt, 1984; Cao et al., 1997; Spiers and Sherratt, 1997).”
BackgroundMethodInfluentialSelf-citationPsoralen Cross-Linking as Probe of Torsional Tension and Topological Domain Sizein Vivo
Sinden, R. R., Bat, O., & Kramer, P. R. (1999) · Methods · doi:10.1006/meth.1998.0723 · Cited by 22
Karaivanova, I. M., Weigel, P., Takahashi, M., Fort, C., Versavaud, A., Duyne, G. D. V., Charlier, D., Hallet, J. N., Glansdorff, N., & Sakanyan, V. A. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3016 · Cited by 21
A pot‐pourri of plasmid paradoxes: effects of a second copy
Yarmolinsky, M. B. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.02127.x · Cited by 21
“The assembly of the complex on a dimer involves resolvase proteins XerC and XerD and accessory proteins ArgR (a repressor of arginine biosynthesis genes) and PepA (an exo-peptidase involved in pyrimidine metabolism) (Guhathakurta and Summers, 1995; Colloms et al., 1996).”
BackgroundDNA sequence of recombinase‐binding sites can determine Xer site‐specific recombination outcome
Blake, J. A. R., Ganguly, N., & Sherratt, D. J. (1997) · Molecular Microbiology · doi:10.1046/j.1365-2958.1997.2261600.x · Cited by 21
“coli K-12 used in this study were all derivatives of AB1157 (Bachmann, 1972): DS941 is recF143 lacZ DM15lacI ; DS956 is DS941 xerA9 (argR::fol ); DS957 is DS941 pepA::Tn5; DS981 is DS941 xerC2 (xerC::kan ); and DS9008 is DS941 xerD2 (xerD::Tn10-9) (Blakely et al., 1993; Colloms et al., 1996).”
BackgroundMethodInfluentialSelf-citationYano, H., Genka, H., Ohtsubo, Y., Nagata, Y., Top, E. M., & Tsuda, M. (2012) · Plasmid · doi:10.1016/j.plasmid.2012.07.004 · Cited by 20
Pedersen, I. B., Helgesen, E., Flåtten, I., Fossum‐Raunehaug, S., & Skarstad, K. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx263 · Cited by 20
“MG1655 Wild type (80,81) AB1157 Wild type (82) MG1655oriCm3 oriCm3 (43) IBP05 oriCm3cam This work UF340 seqA2 (20) UF301 seqA4 dam13 (20) CAG18433 asnB3057::Tn10 (83) SF169 UF301 asnB3057::Tn10 UF301 x P1 CAG18433 N1331 Wild type (84) N1332 recA Ts (80,81,84) NL40 DS941dif 6::KmR (85) DS984 DS941xerC::mini-Mu CmR (86)…”
Relating primary structure to function in the Escherichia coli XerD site‐specific recombinase
Spiers, A. J., & Sherratt, D. J. (1997) · Molecular Microbiology · doi:10.1046/j.1365-2958.1997.4171784.x · Cited by 20
“Substitution of XerD with the catalytically inactive Y279F mutation results in the formation of Holliday junction intermediates as the first pair of strand exchanges is mediated by XerC (Colloms et al., 1996).”
BackgroundMethodInfluentialSelf-citationStrand Selection by the Tyrosine Recombinases
Lee, L., & Sadowski, P. D. (2005) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(05)80001-7 · Cited by 19
Pham, H., Dery, K. J., Sherratt, D. J., & Tolmasky, M. E. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.6.1607-1616.2002 · Cited by 19
“It has been shown before that at a high concentration of PepA, the in vitro recombination reaction at cer could occur in the absence of ArgR (15).”
BackgroundInfluentialSelf-citationDNA Site-Specific Resolution Systems
Hallet, B., Vanhooff, V., & Cornet, F. (2014) · ASM Press eBooks · doi:10.1128/9781555817732.ch7 · Cited by 19
Li, P. (2010) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.1003.03007 · Cited by 19
Bui, D., Ramiscal, J. A. B., Trigueros, S., Newmark, J., Do, A., Sherratt, D. J., & Tolmasky, M. E. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.8.2812-2820.2006 · Cited by 19
“The proteins PepA and ArgR (in the case of cer and mwr) or PepA and ArcA (in the case of psi) bind the accessory sequences and induce the formation of a synaptic complex required for recombination and for ensuring that the reaction is exclusively intramolecular (1, 12, 17, 18, 27, 35).”
BackgroundSelf-citationSwitching catalytic activity in the XerCD site-specific recombination machine 1 1Edited by J. Karn
Ferreira, H., Sherratt, D. J., & Arciszewska, L. K. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4940 · Cited by 19
Self-citationGene Acquisition in Bacteria by Integron‐Mediated Site‐Specific Recombination
Recchia, G. D., & Sherratt, D. J. (2007) · doi:10.1128/9781555817954.ch9 · Cited by 19
Self-citationQuantifying complexity in DNA structures with high resolution Atomic Force Microscopy
Holmes, E. P., Gamill, M. C., Provan, J. I., Wiggins, L., Rusková, R., Whittle, S., Catley, T. E., Main, K. H. S., Shephard, N., Bryant, H. E., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-60559-x · Cited by 18
Self-citationBischerour, J., Spangenberg, C., & Barre, F. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.219 · Cited by 18
“Recombination events are also initiated by XerC during plasmid dimer resolution (Colloms et al , 1996).”
Homology-dependent interactions determine the order of strand exchange by IntDOT recombinase
Laprise, J., Yoneji, S., & Gardner, J. F. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp927 · Cited by 18
Kobryn, K., Briffotaux, J., & Karpov, V. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06584.x · Cited by 18
“…et al., 2002) and there are examples of tyrosine recombinase systems where the HJ is the final product of the recombinase; the HJ is subsequently resolved by other cellular functions into recombinants (i.e. XerC/D acting on cer sites in ColE1 plasmids: McCulloch et al., 1994; Colloms et al., 1996).”
BackgroundPaul, S., & Summers, D. (2004) · Plasmid · doi:10.1016/j.plasmid.2004.04.003 · Cited by 18
Collis, C. M., & Hall, R. M. (2004) · Microbiology · doi:10.1099/mic.0.26596-0 · Cited by 18
“By analogy with the XerCD system (Colloms et al., 1996), strand exchange on the complementary strand seems more likely.”
Simple topology: FtsK-directed recombination at the dif site
Grainge, I. (2013) · Biochemical Society Transactions · doi:10.1042/bst20120299 · Cited by 17
Functional Analysis of the C-terminal Domains of the Site-specific Recombinases XerC and XerD
Ferreira, H., Butler-Cole, B. F. C., Burgin, A. B., Baker, R., Sherratt, D. J., & Arciszewska, L. K. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00558-8 · Cited by 15
Self-citation
Metadata
- Authors
- Colloms, S. D., McCulloch, R., Grant, K., Neilson, L., & Sherratt, D. J.
- Affiliations
- University of Oxford (GB)
- Venue
- The EMBO Journal
- Published
- 1996-03-01
- Volume
- 15
- Issue
- 5
- Pages
- 1172-1181
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC450016
- OpenAlex
- W1538904365
- Cited by
- 136
- References
- 43
- Citations by year
- 2026: 2 · 2025: 3 · 2023: 2 · 2022: 2 · 2020: 4 · 2019: 1 · 2017: 2 · 2016: 1 · 2015: 3 · 2014: 5 · 2013: 3 · 2012: 5
- FWCI
- 8.01
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
- Funders
- Wellcome Trust
- Nuffield Foundation
- Medical Research Council
- Biotechnology and Biological Sciences Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › CRISPR and Genetic Engineering
- Keywords
- XerC, XerD, ArgR, PEPA, plasmid replication, negative supercoiling, Holliday junction, strand exchange, intramolecular recombination
- MeSH terms
- Base Sequence, Binding Sites, DNA Nucleotidyltransferases, DNA, Superhelical, Escherichia coli, Molecular Sequence Data, Nucleic Acid Conformation, Plasmids, Recombination, Genetic, Substrate Specificity, Integrases, Escherichia coli Proteins, Recombinases
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