A computational analysis on the specificity of interactions between histidine kinases and response regulators.
Bacteria process and transmit signals simultaneously through several two-component/phosphorelay networks using closely related proteins. Therefore discrimination against mismatches and discrete recognition between protein partners is an absolute requirement for producing the correct responses. We tried to address this issue by comparing and analyzing sequences from the helix-bundle regions of histidine kinases of Bacillus subtilis. Our analysis shows how conservation and variability in the sequences give rise to selective association and unique recognition. The observed pattern suggests that the chances for cross talk between non-partner proteins are extremely low, but cross talk could take place in special cases.
Mukhopadhyay
Debashis
D
Division of Cellular Biology, Department of Molecular and Experimental Medicine, MEM-116, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
Varughese
Kottayil I
KI
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology; D003198:Computer Simulation; D000071677:Histidine Kinase; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011494:Protein Kinases / Q000378:metabolism*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D014157:Transcription Factors / Q000378:metabolism*
D014157:Transcription Factors; D011494:Protein Kinases; D000071677:Histidine Kinase