Difference between revisions of "RecO"
| Line 81: | Line 81: | ||
* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
** [[SsbA]]-[[RecO]] {{PubMed|21170359}} | ** [[SsbA]]-[[RecO]] {{PubMed|21170359}} | ||
| + | ** [[RecR]]-[[RecO]], [[RecR]]:[[RecO]] molecular ratio of 2:1 (as judged from other bacteria such as ''E. coli'' and ''Deinococcus radiodurans'') {{PubMed|17581636}} | ||
* '''[[Localization]]:''' cytoplasm (according to Swiss-Prot) | * '''[[Localization]]:''' cytoplasm (according to Swiss-Prot) | ||
| Line 86: | Line 87: | ||
=== Database entries === | === Database entries === | ||
| − | * '''Structure:''' | + | * '''Structure:''' |
| + | ** [http://www.rcsb.org/pdb/explore/explore.do?structureId=2V1C 2V1C] (the [[RecR]]-[[RecO]] complex from ''Deinococcus radiodurans'', [[RecR]]: 52% identity, 78% similarity, [[RecO]]: 30%/ 58%) {{PubMed|17581636}} | ||
* '''UniProt:''' [http://www.uniprot.org/uniprot/P42095 P42095] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P42095 P42095] | ||
| Line 128: | Line 130: | ||
=References= | =References= | ||
'''Additional publications:''' {{PubMed|21170359}} | '''Additional publications:''' {{PubMed|21170359}} | ||
| − | <pubmed>,18599486, 19730681 20581116 22373918 </pubmed> | + | <pubmed>,18599486, 19730681 20581116 22373918 17581636</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 15:11, 6 March 2012
- Description: mediator of RecA binding to ssDNA
| Gene name | recO |
| Synonyms | yqxN, yqfI |
| Essential | no |
| Product | mediator of RecA binding to ssDNA |
| Function | DNA repair/ recombination |
| Interactions involving this protein in SubtInteract: RecO | |
| MW, pI | 29 kDa, 8.208 |
| Gene length, protein length | 765 bp, 255 aa |
| Immediate neighbours | glyQ, era |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU25280
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: recO family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P42095
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Additional publications: PubMed
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)
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)
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)
Candela Manfredi, Begoña Carrasco, Silvia Ayora, Juan C Alonso
Bacillus subtilis RecO nucleates RecA onto SsbA-coated single-stranded DNA.
J Biol Chem: 2008, 283(36);24837-47
[PubMed:18599486]
[WorldCat.org]
[DOI]
(P p)
Joanna Timmins, Ingar Leiros, Sean McSweeney
Crystal structure and mutational study of RecOR provide insight into its mode of DNA binding.
EMBO J: 2007, 26(13);3260-71
[PubMed:17581636]
[WorldCat.org]
[DOI]
(P p)
