A regulatory switch involving a Clp ATPase.
Clp ATPase chaperone proteins are found in procaryotes and eucaryotes. Recently, ClpC of Bacillus subtilis was found to be part of a regulatory switch(1). ClpC, in combination with the MecA and ComS proteins, regulates the activity of a transcription factor, ComK, which is necessary for the development of genetic competence (the ability to bind and take up exogenous DNA). The complex of ClpC:MecA:ComK renders ComK inactive. Interaction between ComS and the ternary complex releases active ComK. This regulatory switch controls ComK activity in response to cell density signals that affect production of ComS. Regulated interaction between Clp ATPase and target proteins might prove to be widespread.
Lazazzera
B A
BA
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139, USA.
Grossman
A D
AD
D000251:Adenosine Triphosphatases / Q000235:genetics* / Q000378:metabolism; D000818:Animals; D001412:Bacillus subtilis; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D049071:Endopeptidase Clp; D015964:Gene Expression Regulation, Bacterial; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D012697:Serine Endopeptidases / Q000235:genetics* / Q000378:metabolism
D001426:Bacterial Proteins; C093539:ComS protein, Bacillus subtilis; C083616:mecA protein, Bacillus subtilis; D012697:Serine Endopeptidases; D049071:Endopeptidase Clp; D000251:Adenosine Triphosphatases