@article{FerrandoMay1993methy-18257,
  year={1993},
  title={The methyl-accepting transducer protein Htrl is functionally associated with the photoreceptor sensory rhodopsin I in the archaeon Halobacterium salinarium},
  number={8},
  volume={12},
  journal={The EMBO Journal},
  pages={2999--3005},
  author={Ferrando-May, Elisa and Krah, Monika and Marwan, Wolfgang and Oesterhelt, Dieter}
}

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    <dc:contributor>Krah, Monika</dc:contributor>
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    <dc:contributor>Marwan, Wolfgang</dc:contributor>
    <dc:creator>Ferrando-May, Elisa</dc:creator>
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    <dcterms:title>The methyl-accepting transducer protein Htrl is functionally associated with the photoreceptor sensory rhodopsin I in the archaeon Halobacterium salinarium</dcterms:title>
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    <dc:contributor>Oesterhelt, Dieter</dc:contributor>
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    <dc:creator>Krah, Monika</dc:creator>
    <dc:creator>Marwan, Wolfgang</dc:creator>
    <dcterms:bibliographicCitation>First publ. in: The EMBO Journal ; 12 (1993), 8. -  pp. 2999-3005</dcterms:bibliographicCitation>
    <dcterms:issued>1993</dcterms:issued>
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    <dcterms:abstract xml:lang="eng">We have investigated the functional relationship between two proteins involved in the photosensory system of the archaeon Halobacterium salinarium: the photoreceptor sensory rhodopsin I (SRI) and the halobacterial transducer rhodopsin I (HtrI), which has been proposed to be the putative signal transducer of SRI, by genomic DNA analysis of two independent SRI negative mutants, Pho8l and Dl. Southern and PCR analyses revealed that both strains bear alterations in the 5' flanking region of the gene encoding SRI, sopI. DNA sequence analysis confirmed the occurrence in this region of htrl, the gene encoding the putative transducer protein. PCR and Northern analyses have shown further that sopl and htrl are expressed as a single transcriptional unit, thus explaining the lack of SRI in mutants with a defective htrl. Expression of the cloned sopl under the control of a heterologous promoter did not restore the SRIdependent photoresponse in the strain Pho8l. Moreover, the photocycling rate of the expressed pigment was clearly lower than in wild type. HtrI is therefore essential for SRI function and most likely modulates the photochemical properties of the photoreceptor via direct physical interaction. Finally, reintroduction of both sopI and htrl into Pho8l and Dl restored the SRI photochenistry and its physiological function. Our results provide the first experimental evidence for the functionalcoupling between SRI and HtrI and corroborate the proposed model in which HtrI acts as the signal transducer of this archaeal seven-helix photoreceptor in a way analogous to the bacterial chemotaxis transducers.</dcterms:abstract>
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    <dc:contributor>Ferrando-May, Elisa</dc:contributor>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-03-22T10:35:05Z</dc:date>
    <dc:creator>Oesterhelt, Dieter</dc:creator>
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