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.

[1]  J. Sambrook,et al.  Molecular Cloning: A Laboratory Manual , 2001 .

[2]  Stefan Dipl.-Ing. Schuster,et al.  Phosphorylation in halobacterial signal transduction. , 1995, The EMBO journal.

[3]  M. Engelhard,et al.  The primary structure of sensory rhodopsin II: a member of an additional retinal protein subgroup is coexpressed with its transducer, the halobacterial transducer of rhodopsin II. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[4]  J. Rudolph,et al.  Chemotaxis and phototaxis require a CheA histidine kinase in the archaeon Halobacterium salinarium. , 1995, The EMBO journal.

[5]  Wolfgang Marwan,et al.  A cytoplasmic domain is required for the functional interaction of SRI and HtrI in archaeal signal transduction , 1994, FEBS letters.

[6]  D. Oesterhelt,et al.  Phototaxis of Halobacterium salinarium requires a signalling complex of sensory rhodopsin I and its methyl‐accepting transducer HtrI. , 1994, The EMBO journal.

[7]  D. Oesterhelt,et al.  The methyl‐accepting transducer protein HtrI is functionally associated with the photoreceptor sensory rhodopsin I in the archaeon Halobacterium salinarium. , 1993, The EMBO journal.

[8]  J. Soppa Compilation of Halobacterial Protein Coding Genes, the Halobacterial Codon Usage Table and its Use , 1993 .

[9]  J. Spudich,et al.  Primary structure of an archaebacterial transducer, a methyl-accepting protein associated with sensory rhodopsin I. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[10]  M. Alam,et al.  Structural features of methyl-accepting taxis proteins conserved between archaebacteria and eubacteria revealed by antigenic cross-reaction , 1991, Journal of bacteriology.

[11]  M Lebert,et al.  Methyl‐accepting taxis proteins in Halobacterium halobium. , 1989, The EMBO journal.

[12]  C. A. Hasselbacher,et al.  Methyl-accepting protein associated with bacterial sensory rhodopsin I , 1988, Journal of bacteriology.

[13]  L. Hood,et al.  Immunology: The growing immunoglobulin gene superfamily , 1986, Nature.

[14]  C DeLisi,et al.  The detection and classification of membrane-spanning proteins. , 1985, Biochimica et biophysica acta.

[15]  R. Doolittle,et al.  A simple method for displaying the hydropathic character of a protein. , 1982, Journal of molecular biology.

[16]  J. S. Parkinson,et al.  Communication modules in bacterial signaling proteins. , 1992, Annual review of genetics.