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Titolo:
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
Autore:
SEIDEL R; SCHARF B; GAUTEL M; KLEINE K; OESTERHELT D; ENGELHARD M;
Indirizzi:
MAX PLANCK INST MOLEK PHYSIOL,RHEINLANDDAMM 201 D-44139 HEIDELBERG GERMANY MAX PLANCK INST MOLEK PHYSIOL D-44139 HEIDELBERG GERMANY EUROPEAN MOLEC BIOL LAB D-69117 HEIDELBERG GERMANY MAX PLANCK INST BIOCHEM D-82152 MARTINSRIED GERMANY
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 7, volume: 92, anno: 1995,
pagine: 3036 - 3040
SICI:
0027-8424(1995)92:7<3036:TPSOSR>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
LOW-TEMPERATURE SPECTROPHOTOMETRY; NATRONOBACTERIUM-PHARAONIS; SIGNAL TRANSDUCTION; HALOBIUM; RECEPTOR; BACTERIORHODOPSIN; PHOBORHODOPSIN; PHOTOTAXIS; PHOTORECEPTOR; METHYLATION;
Keywords:
ARCHAEA; PHOTOTAXIS AND CHEMOTAXIS; SIGNAL TRANSDUCTION; PHOTORECEPTOR; PHOTORHODOPSIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
41
Recensione:
Indirizzi per estratti:
Citazione:
R. Seidel 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", Proceedings of the National Academy of Sciences of the United Statesof America, 92(7), 1995, pp. 3036-3040

Abstract

The blue-light receptor genes (sopII) of sensory rhodopsin (SR) II,were cloned from two species. the halophilic bacteria Haloarcula vallismortis (vSR-II) and Natronobacterium pharaonis (pSR-II). Upstream of both sopII gene loci, sequences corresponding to the halobacterial transducer of rhodopsin (Htr) IT were recognized. In N. pharaonis, psopII and phtrII are transcribed as a single transcript. Comparison of the amino acid sequences of vHtr-II and pHtr-II with Htr-I and the chemotactic methyl-accepting proteins from Escherichia coli revealed considerable identities in the signal domain and methyl-accepting sites. Similarities with Htr-I in Halobacterium salinarium suggest a common principle in the phototaxis of extreme halophiles. Alignment of all known retinal protein sequences from Archaea identifies both SR-IIs as an additional subgroup of the family. Positions defining the retinal binding site are usually identical with the exception of Met-118 (numbering is according to the bacteriorhodopsin sequence), which might explain the typical blue color shift of SR-II to approximate to 490 nm, In archaealretinal proteins, the function can be deduced from amino acids in positions 85 and 96, Proton pumps are characterized by Asp-85 and Asp-96;chloride pumps by Thr-85 and Ala-96; and sensors by Asp-85 and Tyr-96or Phe-96.

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Documento generato il 04/12/20 alle ore 21:47:49