Cited by 44Bacterial Genetics and BiotechnologyDNA Repair MechanismsCRISPR and Genetic Engineering

Xer Recombination in Escherichia coli

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Cornet, François, Hallet, Bernard, Sherratt, David J.·1997·Journal of Biological Chemistry

Abstract

Xer site-specific recombination functions in maintaining circular replicons in the monomeric state in Escherichia coli. Two recombinases of the bacteriophage lambda integrase family, XerC and XerD, are required for recombination at the chromosomal site, dif, and at a range of plasmid-borne sites. Xer recombination core sites contain the 11-base pair binding sites for each recombinase separated by a 6 to 8-base pair central region. We report that both XerC and XerD act as site-specific type I topoisomerases by relaxing supercoiled plasmids containing a dif site. Relaxation by either XerC or XerD occurs in the absence of the partner recombinase and requires only a single recombination core site. XerC or XerD relaxation activities are completely inhibited by the addition of the partner recombinase, providing that the DNA recognition sequence for the inhibiting partner is present.

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Crossref · 10.1074/jbc.272.35.21927

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  • The 11-kb LIR encoded a tyrosine recombinase that belonged to the integrase family.

    “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<i>Arthrospira platensis</i>: high genome plasticity and genetic diversity (2016) · cites this paper as [43]

    The introductory passage (page unavailable) identifies XerC and XerD as recombinases related to the integrase family and describes the catalytic role of tyrosine. It does not identify an 11-kb LIR or say that such a region encodes a recombinase; its reference to 11-base-pair sites concerns recombinase binding, not an 11-kb region. (LLM, conf=0.85)

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Research works printed but not linked: 5

  1. Nash, H. A. (1996) in Escherichia coli and Salmonella: Cellular and Molecular Biologie (Neidhardt, F. C., Curtiss, R., III, Ingraham, J. L., Lin, E. C. C., Brooks Low, K., Magasanik, B., Reznikoff, W. S., Riley, M., Schaechter, M., and Umbarger, H. E. eds) 2nd Ed., pp. 2363-2376, ASM Press, Washington, D. C.
  2. Kikuchi, Y., and Nash, H. A., (1979) Proc. Natl. Acad. Sci. U. S. A. 76, 3760 -3764
  3. Brown, P. O., and Cozzarelli, N. R. (1981) Proc. Natl. Acad. Sci. U. S. A. 78, 843-847
  4. Sherratt, D. J., Arciszewska, L. K., Blakely, G., Colloms, S. D., Grant, K., Leslie, N., and McCulloch, R. (1995) Phil. Trans. R. Soc. Lond. 347, 37-42
  5. Tecklenburg, M., Naumer, A., Nagappan, O., and Kuempel, P. L. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 1352-1356

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Authors
Cornet, F., Hallet, B., & Sherratt, D. J.
Affiliations
University of Oxford (GB)
Corresponding author
Sherratt, David J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1997-08
Volume
272
Issue
35
Pages
21927-21931
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2053286804
Cited by
44
References
29
Citations by year
2026: 1 · 2025: 5 · 2022: 1 · 2021: 3 · 2020: 1 · 2017: 1 · 2016: 1 · 2015: 1 · 2014: 2 · 2013: 1
FWCI
1.69
Type
journal article
Language
en
Open access
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Digital Access to Libraries (Université catholique de Louvain (UCL), l'Université de Namur (UNamur) and the Université Saint-Louis (USL-B)) (submittedVersion)
Funders
Wellcome Trust
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, Escherichia coli, topoisomerase I, dif site, plasmid maintenance
MeSH terms
Binding Sites, DNA Nucleotidyltransferases, DNA Topoisomerases, Type I, DNA, Bacterial, DNA, Superhelical, Escherichia coli, Nucleic Acid Conformation, Plasmids, Substrate Specificity, Sequence Analysis, DNA, Integrases, Escherichia coli Proteins, Recombinases

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