Difference between revisions of "LexA"

From SubtiWiki
Jump to: navigation, search
(Reviews)
Line 60: Line 60:
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU17850&redirect=T BSU17850]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/lexA.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/lexA.html]
Line 94: Line 95:
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU17850&redirect=T BSU17850]
  
 
* '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=1JHH 1JHH] (from ''E. coli'', S119A mutant, 33% identity, 52% similarity) {{PubMed|11551506}}
 
* '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=1JHH 1JHH] (from ''E. coli'', S119A mutant, 33% identity, 52% similarity) {{PubMed|11551506}}

Revision as of 13:50, 2 April 2014

  • Description: transcriptional repressor of the SOS regulon

Gene name lexA
Synonyms dinR
Essential no
Product transcriptional repressor of the SOS regulon
Function regulation of DNA damage repair
Gene expression levels in SubtiExpress: lexA
Function and regulation of this protein in SubtiPathways:
lexA
MW, pI 22 kDa, 5.155
Gene length, protein length 615 bp, 205 aa
Immediate neighbours fosB, yneA
Sequences Protein DNA DNA_with_flanks
Genetic context
LexA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
LexA expression.png




























Categories containing this gene/protein

DNA repair/ recombination, transcription factors and their control

This gene is a member of the following regulons

LexA regulon

The LexA regulon

The gene

Basic information

  • Locus tag: BSU17850

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Represses uvrB, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. (according to Swiss-Prot)
  • Protein family: peptidase S24 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1JHH (from E. coli, S119A mutant, 33% identity, 52% similarity) PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • Regulatory mechanism: autorepression

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Reviews

Justin S Lenhart, Jeremy W Schroeder, Brian W Walsh, Lyle A Simmons
DNA repair and genome maintenance in Bacillus subtilis.
Microbiol Mol Biol Rev: 2012, 76(3);530-64
[PubMed:22933559] [WorldCat.org] [DOI] (I p)

M Butala, D Zgur-Bertok, S J W Busby
The bacterial LexA transcriptional repressor.
Cell Mol Life Sci: 2009, 66(1);82-93
[PubMed:18726173] [WorldCat.org] [DOI] (I p)


Original publications

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

Yoshikazu Kawai, Naotake Ogasawara
Bacillus subtilis EzrA and FtsL synergistically regulate FtsZ ring dynamics during cell division.
Microbiology (Reading): 2006, 152(Pt 4);1129-1141
[PubMed:16549676] [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)

Y Luo, R A Pfuetzner, S Mosimann, M Paetzel, E A Frey, M Cherney, B Kim, J W Little, N C Strynadka
Crystal structure of LexA: a conformational switch for regulation of self-cleavage.
Cell: 2001, 106(5);585-94
[PubMed:11551506] [WorldCat.org] [DOI] (P p)

K W Winterling, D Chafin, J J Hayes, J Sun, A S Levine, R E Yasbin, R Woodgate
The Bacillus subtilis DinR binding site: redefinition of the consensus sequence.
J Bacteriol: 1998, 180(8);2201-11
[PubMed:9555905] [WorldCat.org] [DOI] (P p)

K W Winterling, A S Levine, R E Yasbin, R Woodgate
Characterization of DinR, the Bacillus subtilis SOS repressor.
J Bacteriol: 1997, 179(5);1698-703
[PubMed:9045831] [WorldCat.org] [DOI] (P p)

M C Miller, J B Resnick, B T Smith, C M Lovett
The bacillus subtilis dinR gene codes for the analogue of Escherichia coli LexA. Purification and characterization of the DinR protein.
J Biol Chem: 1996, 271(52);33502-8
[PubMed:8969214] [WorldCat.org] (P p)

B J Haijema, D van Sinderen, K Winterling, J Kooistra, G Venema, L W Hamoen
Regulated expression of the dinR and recA genes during competence development and SOS induction in Bacillus subtilis.
Mol Microbiol: 1996, 22(1);75-85
[PubMed:8899710] [WorldCat.org] [DOI] (P p)

A Raymond-Denise, N Guillen
Identification of dinR, a DNA damage-inducible regulator gene of Bacillus subtilis.
J Bacteriol: 1991, 173(22);7084-91
[PubMed:1657879] [WorldCat.org] [DOI] (P p)