Open AccessA family of halobacterial transducer proteins
Author(s) -
Rudolph Johannes,
Nordmann Barbara,
Storch KaiFlorian,
Gruenberg Heidi,
Rodewald Karin,
Oesterhelt Dieter
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08197.x
Subject(s) - phototaxis , biology , chemotaxis , halobacterium , homology (biology) , transmembrane domain , transmembrane protein , signal transduction , biochemistry , microbiology and biotechnology , genetics , amino acid , bacteriorhodopsin , receptor , membrane
A DNA probe to the signaling domain of a halobacterial transducer for phototaxis (HtrI) was used to clone and sequence four members of a new family of transducer proteins (Htps) in Halobacterium salinarium potentially involved in chemo‐ or phototactic signal transduction. The signaling domains in these proteins have 31–43% identity when compared with each other or with their bacterial analogs, the methyl‐accepting chemotaxis proteins. An additional region of homology found in three of the Htps has 31–43% identity with Htrl. The Htps contain from 0 to 3 transmembrane helices and Western blotting showed that HtpIII is soluble. The arrangement of the domains in these Htps suggests a modular architecture in their construction.