A phylogenomic study of the general stress response sigma factor sigmaB of Bacillus subtilis and its regulatory proteins.
Regulation of expression of the general stress regulon of Bacillus subtilis is mediated by the activation of the alternative sigma factor sigmaB. Activation of sigmaB is accomplished by a complex regulatory network involving protein-protein interactions and reversible protein phosphorylation. PSI-BLAST searches were performed and phylogenetic trees for sigmaB and its regulatory proteins were constructed. Occurrence of sigmaB is restricted to a small group of gram-positive bacteria (Bacillus, Staphylococcus, Listeria). Related sigma factors also involved in stress responses are present in Mycobacterium tuberculosis, Streptomyces species and even in cyanobacteria (Synechocystis species). Putative regulatory proteins found in several other bacterial species can be broadly catagorized into three categories: Anti sigma factors, anti-anti sigma factors and phosphatases. Anti sigma factors are able to bind to sigma factors and are also kinases of anti sigma factor antagonists. Only in their nonphosphorylated state, these antagonists are able to bind to the anti sigma factor. Phosphorylated antagonists can be dephosphorylated by PP2C phosphatases. These phosphatases are of pivotal importance for activation of the sigma factor. Different phosphatases identified in this search contain a wide variety of domains found in signal transducing proteins (PAS/PAC, GAF, REC, HATase_c, HAMP). The HATPase_c domain found in several phosphatases most probably constitutes a serine/threonine kinase domain of anti sigma factors. Such proteins are most probably bifunctional anti-anti sigma factor kinases and phosphatases. The regulatory network of anti-anti sigma factors anti sigma factors and phosphatases is probably ancient and most likely evolved from a structurally similar network found in the Deinococcus radiodurans genome. In completely sequenced genomes of several bacterial species, some elements of the network are missing. The N-terminus of RsbU, a phosphatase activated in response to environmental stress exhibits similarities to a region in the beta chain of phenylalanyl-tRNA synthetases.
Gerhard.Mittenhuber@biologie.uni-greifswald.de
Gerhard
G
Mittenhuber
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000145:classification / Q000235:genetics*; D001426:Bacterial Proteins / Q000235:genetics*; D006090:Gram-Negative Bacteria / Q000235:genetics; D008969:Molecular Sequence Data; D010652:Phenylalanine-tRNA Ligase / Q000235:genetics; D010766:Phosphorylation; D010802:Phylogeny; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012808:Sigma Factor / Q000235:genetics*; D014157:Transcription Factors / Q000235:genetics*
D001426:Bacterial Proteins; C079011:SigB protein, Bacteria; D012808:Sigma Factor; D014157:Transcription Factors; D010652:Phenylalanine-tRNA Ligase