Difference between revisions of "SsbA"

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(→‎Extended information on the protein)
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** [[SsbA]]-[[Ung]] {{PubMed|21170359}}
 
** [[SsbA]]-[[Ung]] {{PubMed|21170359}}
 
** [[SsbA]]-[[YpbB]] {{PubMed|21170359}}
 
** [[SsbA]]-[[YpbB]] {{PubMed|21170359}}
−
** [[SsbA]]-[[RecD2]] {{PubMed|21170359}}
+
** [[SsbA]]-[[RecD2]] {{PubMed|24443534,21170359}}
 
** [[SsbA]]-[[DnaN]]  {{PubMed|21958350}}
 
** [[SsbA]]-[[DnaN]]  {{PubMed|21958350}}
 
** [[SsbA]] (bound to ssDNA) -[[RecO]], this helps to dislodge [[SsbA]] and [[SsbB]] from ssDNA {{PubMed|21170359,22373918}}
 
** [[SsbA]] (bound to ssDNA) -[[RecO]], this helps to dislodge [[SsbA]] and [[SsbB]] from ssDNA {{PubMed|21170359,22373918}}
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<pubmed> 22976189 22933559 </pubmed>
 
<pubmed> 22976189 22933559 </pubmed>
 
== Original publications ==
 
== Original publications ==
−
<pubmed>17853894,19730681 11948146,16479537,11948165 16549871 20122408 14762004 20581116 22054219 22373918 22517742 21859751, 21170359, 21958350,23268446 23536821 23779106 22383849 24310371 </pubmed>
+
<pubmed>17853894,19730681 11948146,16479537,11948165 16549871 20122408 14762004 20581116 22054219 22373918 22517742 21859751, 21170359, 21958350,23268446 23536821 23779106 22383849 24310371 24443534</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 17:51, 22 January 2014

  • Description: single-strand DNA-binding protein, part of the replisome

Gene name ssbA
Synonyms ssb
Essential yes PubMed
Product single-strand DNA-binding protein
Function DNA replication, DNA repair/ recombination
Gene expression levels in SubtiExpress: ssbA
Interactions involving this protein in SubtInteract: SsbA
MW, pI 18 kDa, 4.822
Gene length, protein length 516 bp, 172 aa
Immediate neighbours rpsR, rpsF
Sequences Protein DNA DNA_with_flanks
Genetic context
Ssb context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SsbA expression.png















Categories containing this gene/protein

DNA replication, DNA repair/ recombination, essential genes, phosphoproteins

This gene is a member of the following regulons

ComK regulon, stringent response

The gene

Basic information

  • Locus tag: BSU40900

Phenotypes of a mutant

essential PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • SsbA inhibits ssDNA phosphorylase activity of PnpA PubMed
    • SsbA co-assembles onto SsbB-coated ssDNA PubMed
  • Protein family:
  • Paralogous protein(s): SsbB

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity: Phosphorylation of Ssb increases binding to single-stranded DNA in vitro almost 200-fold PubMed

Database entries

  • Structure: 3VDY 3VDY (SsbB in complex with ssDNA, 63% identity, 87% similarity) PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
    • ComK: transcription activation PubMed
  • Additional information:
    • the mRNA contains a structured motif in the 5' UTR upstream of the rpsF ORF that is bound by RpsF-RpsR heterodimers and may be implicated in autogenous regulation PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Original publications

Brian W Walsh, Samantha A Bolz, Sarah R Wessel, Jeremy W Schroeder, James L Keck, Lyle A Simmons
RecD2 helicase limits replication fork stress in Bacillus subtilis.
J Bacteriol: 2014, 196(7);1359-68
[PubMed:24443534] [WorldCat.org] [DOI] (I p)

Yang Fu, Kaila Deiorio-Haggar, Mark W Soo, Michelle M Meyer
Bacterial RNA motif in the 5' UTR of rpsF interacts with an S6:S18 complex.
RNA: 2014, 20(2);168-76
[PubMed:24310371] [WorldCat.org] [DOI] (I p)

Tribhuwan Yadav, Begoña Carrasco, James Hejna, Yuki Suzuki, Kunio Takeyasu, Juan C Alonso
Bacillus subtilis DprA recruits RecA onto single-stranded DNA and mediates annealing of complementary strands coated by SsbB and SsbA.
J Biol Chem: 2013, 288(31);22437-50
[PubMed:23779106] [WorldCat.org] [DOI] (I p)

Aimee H Marceau, Douglas A Bernstein, Brian W Walsh, Walker Shapiro, Lyle A Simmons, James L Keck
Protein interactions in genome maintenance as novel antibacterial targets.
PLoS One: 2013, 8(3);e58765
[PubMed:23536821] [WorldCat.org] [DOI] (I p)

Elena M Seco, John C Zinder, Carol M Manhart, Ambra Lo Piano, Charles S McHenry, Silvia Ayora
Bacteriophage SPP1 DNA replication strategies promote viral and disable host replication in vitro.
Nucleic Acids Res: 2013, 41(3);1711-21
[PubMed:23268446] [WorldCat.org] [DOI] (I p)

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

Tribhuwan Yadav, Begoña Carrasco, Angela R Myers, Nicholas P George, James L Keck, Juan C Alonso
Genetic recombination in Bacillus subtilis: a division of labor between two single-strand DNA-binding proteins.
Nucleic Acids Res: 2012, 40(12);5546-59
[PubMed:22373918] [WorldCat.org] [DOI] (I p)

Wei Zhang, Xiujuan Lü, Wenke Zhang, Jiacong Shen
EMSA and single-molecule force spectroscopy study of interactions between Bacillus subtilis single-stranded DNA-binding protein and single-stranded DNA.
Langmuir: 2011, 27(24);15008-15
[PubMed:22054219] [WorldCat.org] [DOI] (I p)

Andrew D Klocko, Jeremy W Schroeder, Brian W Walsh, Justin S Lenhart, Margery L Evans, Lyle A Simmons
Mismatch repair causes the dynamic release of an essential DNA polymerase from the replication fork.
Mol Microbiol: 2011, 82(3);648-63
[PubMed:21958350] [WorldCat.org] [DOI] (I p)

Paula P Cardenas, Thomas Carzaniga, Sandro Zangrossi, Federica Briani, Esther Garcia-Tirado, Gianni Dehò, Juan C Alonso
Polynucleotide phosphorylase exonuclease and polymerase activities on single-stranded DNA ends are modulated by RecN, SsbA and RecA proteins.
Nucleic Acids Res: 2011, 39(21);9250-61
[PubMed:21859751] [WorldCat.org] [DOI] (I p)

Audrey Costes, François Lecointe, Stephen McGovern, Sophie Quevillon-Cheruel, Patrice Polard
The C-terminal domain of the bacterial SSB protein acts as a DNA maintenance hub at active chromosome replication forks.
PLoS Genet: 2010, 6(12);e1001238
[PubMed:21170359] [WorldCat.org] [DOI] (I e)

Candela Manfredi, Yuki Suzuki, Tribhuwan Yadav, Kunio Takeyasu, Juan C Alonso
RecO-mediated DNA homology search and annealing is facilitated by SsbA.
Nucleic Acids Res: 2010, 38(20);6920-9
[PubMed:20581116] [WorldCat.org] [DOI] (I p)

Glenn M Sanders, H Garry Dallmann, Charles S McHenry
Reconstitution of the B. subtilis replisome with 13 proteins including two distinct replicases.
Mol Cell: 2010, 37(2);273-81
[PubMed:20122408] [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)

François Lecointe, Céline Sérèna, Marion Velten, Audrey Costes, Stephen McGovern, Jean-Christophe Meile, Jeffrey Errington, S Dusko Ehrlich, Philippe Noirot, Patrice Polard
Anticipating chromosomal replication fork arrest: SSB targets repair DNA helicases to active forks.
EMBO J: 2007, 26(19);4239-51
[PubMed:17853894] [WorldCat.org] [DOI] (P p)

Ivan Mijakovic, Dina Petranovic, Boris Macek, Tina Cepo, Matthias Mann, Julian Davies, Peter R Jensen, Dusica Vujaklija
Bacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine.
Nucleic Acids Res: 2006, 34(5);1588-96
[PubMed:16549871] [WorldCat.org] [DOI] (I e)

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)

Cordula Lindner, Reindert Nijland, Mariska van Hartskamp, Sierd Bron, Leendert W Hamoen, Oscar P Kuipers
Differential expression of two paralogous genes of Bacillus subtilis encoding single-stranded DNA binding protein.
J Bacteriol: 2004, 186(4);1097-105
[PubMed:14762004] [WorldCat.org] [DOI] (P p)

Christine Eymann, Georg Homuth, Christian Scharf, Michael Hecker
Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis.
J Bacteriol: 2002, 184(9);2500-20
[PubMed:11948165] [WorldCat.org] [DOI] (P p)

Mitsuo Ogura, Hirotake Yamaguchi, Kazuo Kobayashi, Naotake Ogasawara, Yasutaro Fujita, Teruo Tanaka
Whole-genome analysis of genes regulated by the Bacillus subtilis competence transcription factor ComK.
J Bacteriol: 2002, 184(9);2344-51
[PubMed:11948146] [WorldCat.org] [DOI] (P p)

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