LexA repressor

LexA DNA binding domain
lexa s119a mutant
Identifiers
SymbolLexA_DNA_bind
PfamPF01726
Pfam clanCL0123
InterProIPR006199
SCOP21leb / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

The LexA repressor or LexA (Locus for X-ray sensitivity A)[1] is a transcriptional repressor (EC 3.4.21.88) that represses SOS response genes coding primarily for error-prone DNA polymerases, DNA repair enzymes and cell division inhibitors.[2] LexA forms de facto a two-component regulatory system with RecA, which senses DNA damage at stalled replication forks, forming monofilaments and acquiring an active conformation capable of binding to LexA and causing LexA to cleave itself, in a process called autoproteolysis.[1]

LexA polypeptides contains a two domains: a DNA-binding domain and a dimerization domain.[3] The dimerization domain binds to other LexA polypeptides to form dumbbell shaped dimers. The DNA-binding domain is a variant form of the helix-turn-helix DNA binding motif,[4] and is usually located at the N-terminus of the protein.[1] This domain is bound to an SOS box upstream of SOS response genes until DNA damage stimulates autoproteolysis.[3]

  1. ^ a b c Butala M, Žgur-Bertok D, Busby SJ (January 2009). "The bacterial LexA transcriptional repressor". Cellular and Molecular Life Sciences. 66 (1): 82–93. doi:10.1007/s00018-008-8378-6. PMC 11131485. PMID 18726173. S2CID 29537019.
  2. ^ Erill I, Campoy S, Barbé J (November 2007). "Aeons of distress: an evolutionary perspective on the bacterial SOS response". FEMS Microbiology Reviews. 31 (6): 637–656. doi:10.1111/j.1574-6976.2007.00082.x. PMID 17883408.
  3. ^ a b Henkin TM, Peters JE (2020). "DNA Repair and Mutagenesis". Snyder and Champness molecular genetics of bacteria (Fifth ed.). Hoboken, NJ : Washington, D.C: John Wiley & Sons, Inc. ISBN 9781555819750.
  4. ^ Fogh RH, Ottleben G, Rüterjans H, Schnarr M, Boelens R, Kaptein R (September 1994). "Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy". The EMBO Journal. 13 (17): 3936–3944. doi:10.1002/j.1460-2075.1994.tb06709.x. PMC 395313. PMID 8076591.