Difference between revisions of "RecA"

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|style="background:#ABCDEF;" align="center"| '''Product''' || multifunctional protein involved in homologous <br/>recombination and DNA repair ([[LexA]]-autocleavage)
 
|style="background:#ABCDEF;" align="center"| '''Product''' || multifunctional protein involved in homologous <br/>recombination and DNA repair ([[LexA]]-autocleavage)
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Function''' || genetic [[recombination]], [[DNA repair]]
+
|style="background:#ABCDEF;" align="center"|'''Function''' || [[DNA repair/ recombination]]
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 37 kDa, 4.883   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 37 kDa, 4.883   

Revision as of 12:15, 1 February 2011

  • Description: multifunctional protein involved in homologous recombination and DNA repair (LexA-autocleavage)

Gene name recA
Synonyms recE
Essential no
Product multifunctional protein involved in homologous
recombination and DNA repair (LexA-autocleavage)
Function DNA repair/ recombination
MW, pI 37 kDa, 4.883
Gene length, protein length 1041 bp, 347 aa
Immediate neighbours cinA, pbpX
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RecA context.gif
This image was kindly provided by SubtiList




Categories containing this gene/protein

DNA repair/ recombination, genetic competence

This gene is a member of the following regulons

ComK regulon, LexA regulon

The gene

Basic information

  • Locus tag: BSU16940

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

RecA filaments are dismantled from DNA by PcrA PubMed


The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: recA family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylated on Ser-2 PubMed
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:
    • cytoplasm (according to Swiss-Prot)
    • Nucleoid (Mid-cell) PubMed
    • localizes to one cell pole PubMed

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • induced by DNA damage (LexA) PubMed
    • induced by conditions that trigger development of genetic competence (ComK) PubMed
  • Additional information:

Biological materials

  • Mutant: IRN444 (cat), available in the Stülke lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Peter Graumann, Freiburg University, Germany homepage

Your additional remarks

References

Reviews

Justin Courcelle, Philip C Hanawalt
RecA-dependent recovery of arrested DNA replication forks.
Annu Rev Genet: 2003, 37;611-46
[PubMed:14616075] [WorldCat.org] [DOI] (P p)

Michael M Cox
The bacterial RecA protein as a motor protein.
Annu Rev Microbiol: 2003, 57;551-77
[PubMed:14527291] [WorldCat.org] [DOI] (P p)

Shelley L Lusetti, Michael M Cox
The bacterial RecA protein and the recombinational DNA repair of stalled replication forks.
Annu Rev Biochem: 2002, 71;71-100
[PubMed:12045091] [WorldCat.org] [DOI] (P p)

M M Cox
Recombinational DNA repair in bacteria and the RecA protein.
Prog Nucleic Acid Res Mol Biol: 1999, 63;311-66
[PubMed:10506835] [WorldCat.org] [DOI] (P p)

Original publications

Miriam Kaufenstein, Martin van der Laan, Peter L Graumann
The three-layered DNA uptake machinery at the cell pole in competent Bacillus subtilis cells is a stable complex.
J Bacteriol: 2011, 193(7);1633-42
[PubMed:21278288] [WorldCat.org] [DOI] (I p)

Jeehae Park, Sua Myong, Anita Niedziela-Majka, Kyung Suk Lee, Jin Yu, Timothy M Lohman, Taekjip Ha
PcrA helicase dismantles RecA filaments by reeling in DNA in uniform steps.
Cell: 2010, 142(4);544-55
[PubMed:20723756] [WorldCat.org] [DOI] (I p)

Boumediene Soufi, Chanchal Kumar, Florian Gnad, Matthias Mann, Ivan Mijakovic, Boris Macek
Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis.
J Proteome Res: 2010, 9(7);3638-46
[PubMed:20509597] [WorldCat.org] [DOI] (I p)

Dawit Kidane, Begoña Carrasco, Candela Manfredi, Katharina Rothmaier, Silvia Ayora, Serkalem Tadesse, Juan C Alonso, Peter L Graumann
Evidence for different pathways during horizontal gene transfer in competent Bacillus subtilis cells.
PLoS Genet: 2009, 5(9);e1000630
[PubMed:19730681] [WorldCat.org] [DOI] (I p)

Lyle A Simmons, Alexi I Goranov, Hajime Kobayashi, Bryan W Davies, Daniel S Yuan, Alan D Grossman, Graham C Walker
Comparison of responses to double-strand breaks between Escherichia coli and Bacillus subtilis reveals different requirements for SOS induction.
J Bacteriol: 2009, 191(4);1152-61
[PubMed:19060143] [WorldCat.org] [DOI] (I p)

Isabelle Mortier-Barrière, Marion Velten, Pauline Dupaigne, Nicolas Mirouze, Olivier Piétrement, Stephen McGovern, Gwennaele Fichant, Bernard Martin, Philippe Noirot, Eric Le Cam, Patrice Polard, Jean-Pierre Claverys
A key presynaptic role in transformation for a widespread bacterial protein: DprA conveys incoming ssDNA to RecA.
Cell: 2007, 130(5);824-36
[PubMed:17803906] [WorldCat.org] [DOI] (P p)

Naomi Kramer, Jeanette Hahn, David Dubnau
Multiple interactions among the competence proteins of Bacillus subtilis.
Mol Microbiol: 2007, 65(2);454-64
[PubMed:17630974] [WorldCat.org] [DOI] (P p)

Syam P Anand, Haocheng Zheng, Piero R Bianco, Sanford H Leuba, Saleem A Khan
DNA helicase activity of PcrA is not required for the displacement of RecA protein from DNA or inhibition of RecA-mediated strand exchange.
J Bacteriol: 2007, 189(12);4502-9
[PubMed:17449621] [WorldCat.org] [DOI] (P p)

Lyle A Simmons, Alan D Grossman, Graham C Walker
Replication is required for the RecA localization response to DNA damage in Bacillus subtilis.
Proc Natl Acad Sci U S A: 2007, 104(4);1360-5
[PubMed:17229847] [WorldCat.org] [DOI] (P p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

Nora Au, Elke Kuester-Schoeck, Veena Mandava, Laura E Bothwell, Susan P Canny, Karen Chachu, Sierra A Colavito, Shakierah N Fuller, Eli S Groban, Laura A Hensley, Theresa C O'Brien, Amish Shah, Jessica T Tierney, Louise L Tomm, Thomas M O'Gara, Alexi I Goranov, Alan D Grossman, Charles M Lovett
Genetic composition of the Bacillus subtilis SOS system.
J Bacteriol: 2005, 187(22);7655-66
[PubMed:16267290] [WorldCat.org] [DOI] (P p)

Dawit Kidane, Peter L Graumann
Dynamic formation of RecA filaments at DNA double strand break repair centers in live cells.
J Cell Biol: 2005, 170(3);357-66
[PubMed:16061691] [WorldCat.org] [DOI] (P p)

Begoña Carrasco, Silvia Ayora, Rudi Lurz, Juan C Alonso
Bacillus subtilis RecU Holliday-junction resolvase modulates RecA activities.
Nucleic Acids Res: 2005, 33(12);3942-52
[PubMed:16024744] [WorldCat.org] [DOI] (I e)

Hanne Jarmer, Randy Berka, Steen Knudsen, Hans H Saxild
Transcriptome analysis documents induced competence of Bacillus subtilis during nitrogen limiting conditions.
FEMS Microbiol Lett: 2002, 206(2);197-200
[PubMed:11814663] [WorldCat.org] [DOI] (P p)

L W Hamoen, B Haijema, J J Bijlsma, G Venema, C M Lovett
The Bacillus subtilis competence transcription factor, ComK, overrides LexA-imposed transcriptional inhibition without physically displacing LexA.
J Biol Chem: 2001, 276(46);42901-7
[PubMed:11555642] [WorldCat.org] [DOI] (P p)

C M Lovett, K C Cho, T M O'Gara
Purification of an SOS repressor from Bacillus subtilis.
J Bacteriol: 1993, 175(21);6842-9
[PubMed:8226626] [WorldCat.org] [DOI] (P p)

D L Cheo, K W Bayles, R E Yasbin
Elucidation of regulatory elements that control damage induction and competence induction of the Bacillus subtilis SOS system.
J Bacteriol: 1993, 175(18);5907-15
[PubMed:7690748] [WorldCat.org] [DOI] (P p)