A family of halobacterial transducer proteins.
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 HtrI. 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.
Rudolph
J
J
Max-Planck-Institut for Biochemistry, Martinsried, Germany.
Nordmann
B
B
Storch
K F
KF
Gruenberg
H
H
Rodewald
K
K
Oesterhelt
D
D
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D001483:Base Sequence; D015153:Blotting, Western; D015342:DNA Probes; D006216:Halobacteriaceae / Q000737:chemistry / Q000235:genetics*; D008745:Methylation; D008969:Molecular Sequence Data; D011485:Protein Binding / Q000235:genetics; D011487:Protein Conformation; D015398:Signal Transduction / Q000235:genetics*
D001426:Bacterial Proteins; D015342:DNA Probes