RecBCD Enzyme and the Repair of Double-Stranded DNA Breaks

Dillingham, Mark S.; Kowalczykowski, Stephen C.

doi:10.1128/mmbr.00020-08

Cited by 503 publications

(629 citation statements)

References 329 publications

(448 reference statements)

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“…The targeting to gDNA occurs even in the presence of a 1000-fold excess of ssDNA. The dissociation constant, K d , for RecF protein binding to gDNA in the presence of RecOR proteins was determined to be ϳ1-2 nM, a value that is similar to the K d value of the RecBCD-dsDNA interaction (35). If an E. coli cell contained only 10 molecules of RecF protein, its concentration would be about ϳ10 nM (based on the volume of an E. coli cell of ϳ1 ϫ 10 Ϫ15 liter).…”

Section: Discussionmentioning

confidence: 99%

RecFOR Proteins Target RecA Protein to a DNA Gap with Either DNA or RNA at the 5′ Terminus

Morimatsu

Wu²,

Kowalczykowski

2012

Journal of Biological Chemistry

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Background: Mediator proteins regulate assembly of RecA onto single-stranded DNA complexed with SSB protein.Results: RecFOR targets RecA to the 5Ј-end of DNA gaps, regardless whether terminated by DNA or RNA. Conclusion: RecFOR loads RecA onto RNA-DNA substrates that mimic unfinished lagging strand replication gaps. Significance: This work provides biochemical evidence for recognition by RecF of gaps created when DNA replication halts.

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Section: Discussionmentioning

confidence: 99%

RecFOR Proteins Target RecA Protein to a DNA Gap with Either DNA or RNA at the 5′ Terminus

Morimatsu

Wu²,

Kowalczykowski

2012

Journal of Biological Chemistry

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“…RecBCD functions both in restricting foreign genomes and in host DNA repair by recombination (34). The DNA repair function on the phage genome or the restriction function on host DNA could potentially be lethal to the host.…”

Section: Non-r-m Defense Systemsmentioning

confidence: 99%

Diverse Functions of Restriction-Modification Systems in Addition to Cellular Defense

Vasu

Nagaraja

2013

Microbiol Mol Biol Rev

507

462

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SUMMARY Restriction-modification (R-M) systems are ubiquitous and are often considered primitive immune systems in bacteria. Their diversity and prevalence across the prokaryotic kingdom are an indication of their success as a defense mechanism against invading genomes. However, their cellular defense function does not adequately explain the basis for their immaculate specificity in sequence recognition and nonuniform distribution, ranging from none to too many, in diverse species. The present review deals with new developments which provide insights into the roles of these enzymes in other aspects of cellular function. In this review, emphasis is placed on novel hypotheses and various findings that have not yet been dealt with in a critical review. Emerging studies indicate their role in various cellular processes other than host defense, virulence, and even controlling the rate of evolution of the organism. We also discuss how R-M systems could have successfully evolved and be involved in additional cellular portfolios, thereby increasing the relative fitness of their hosts in the population.

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“…Thus, the well-characterized RMPs UvsY of bacteriophage T4, Rec(F)OR of Escherichia coli, and yeast Rad52 alleviate the SSB barrier and promote the loading of UvsX, RecA, and Rad51 on Gp32-, SSB-, and RP-Aprecoated ssDNA, respectively (3). The E. coli RecBCD complex represents another category of cofactors that process linear dsDNA into ssDNA onto which they simultaneously ensure the loading of the recombinase (4).…”

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confidence: 99%

Structure–function analysis of pneumococcal DprA protein reveals that dimerization is crucial for loading RecA recombinase onto DNA during transformation

Quevillon‐Chéruel

Campo

Mirouze

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

152

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Transformation promotes genome plasticity in bacteria via RecAdriven homologous recombination. In the Gram-positive human pathogen Streptococcus pneumoniae, the transformasome a multiprotein complex, internalizes, protects, and processes transforming DNA to generate chromosomal recombinants. Double-stranded DNA is internalized as single strands, onto which the transformation-dedicated DNA processing protein A (DprA) ensures the loading of RecA to form presynaptic filaments. We report that the structure of DprA consists of the association of a sterile alpha motif domain and a Rossmann fold and that DprA forms tail-totail dimers. The isolation of DprA self-interaction mutants revealed that dimerization is crucial for the formation of nucleocomplexes in vitro and for genetic transformation. Residues important for DprARecA interaction also were identified and mutated, establishing this interaction as equally important for transformation. Positioning of key interaction residues on the DprA structure revealed an overlap of DprA-DprA and DprA-RecA interaction surfaces. We propose a model in which RecA interaction promotes rearrangement or disruption of the DprA dimer, enabling the subsequent nucleation of RecA and its polymerization onto ssDNA.bacterial transformation | genetic exchange | recombinase loader | recombination mediator protein | horizontal gene transfer

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RecBCD Enzyme and the Repair of Double-Stranded DNA Breaks

Cited by 503 publications

References 329 publications

RecFOR Proteins Target RecA Protein to a DNA Gap with Either DNA or RNA at the 5′ Terminus

RecFOR Proteins Target RecA Protein to a DNA Gap with Either DNA or RNA at the 5′ Terminus

Diverse Functions of Restriction-Modification Systems in Addition to Cellular Defense

Structure–function analysis of pneumococcal DprA protein reveals that dimerization is crucial for loading RecA recombinase onto DNA during transformation

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