Literature DB >> 8674984

A family of halobacterial transducer proteins.

J Rudolph1, B Nordmann, K F Storch, H Gruenberg, K Rodewald, D Oesterhelt.   

Abstract

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.

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Year:  1996        PMID: 8674984     DOI: 10.1111/j.1574-6968.1996.tb08197.x

Source DB:  PubMed          Journal:  FEMS Microbiol Lett        ISSN: 0378-1097            Impact factor:   2.742


  19 in total

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Authors:  K F Storch; J Rudolph; D Oesterhelt
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4.  Primary structure and functional analysis of the soluble transducer protein HtrXI in the archaeon Halobacterium salinarium.

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Review 5.  Posttranslational protein modification in Archaea.

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Journal:  Infect Immun       Date:  1998-06       Impact factor: 3.441

8.  A novel mode of sensory transduction in archaea: binding protein-mediated chemotaxis towards osmoprotectants and amino acids.

Authors:  Maia V Kokoeva; Kai-Florian Storch; Christian Klein; Dieter Oesterhelt
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9.  Protein-protein interaction changes in an archaeal light-signal transduction.

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Journal:  J Biomed Biotechnol       Date:  2010-06-29

10.  Molecular cloning, sequencing, and expression of a chemoreceptor gene from Leptospirillum ferrooxidans.

Authors:  M Delgado; H Toledo; C A Jerez
Journal:  Appl Environ Microbiol       Date:  1998-07       Impact factor: 4.792

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