Document Detail


Identification and characterization of a protostome homologue of peropsin from a jumping spider.
MedLine Citation:
PMID:  19960196     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Peropsin, a member of the opsin family, has characteristics of two functionally distinct opsin-groups, that is, amino acid residues conserved among opsins for light-sensing and a retinal-photoisomerase-like molecular property. Although such a bilateral feature of peropsin seems to be important for understanding the diversity of the opsin family, previous studies have been limited to higher deuterostome, vertebrate and amphioxus peropsins. Here, we report a protostome peropsin homologue from a jumping spider. We found a spider opsin that shares amino acid homology and conserved amino acid residues with known peropsins. The spider opsin-based pigment heterologously expressed in cultured cells exhibited photoisomerase-like isomerization characteristics and a bistable nature. Based on the characteristics of both the amino acid homology and its photochemical properties, we concluded that the spider opsin is the first protostome peropsin homologue. These results show that peropsin existed before the deuterostome-protostome split like other members of the opsin family. In addition, the spider peropsin was localized to non-visual cells in the retina, and fluorescence from reduced retinal chromophore was also observed in the region where peropsin was localized. These findings provide the first demonstration that the peropsin can form a photosensitive pigment in vivo and underlie non-visual function.
Authors:
Takashi Nagata; Mitsumasa Koyanagi; Hisao Tsukamoto; Akihisa Terakita
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-12-04
Journal Detail:
Title:  Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology     Volume:  196     ISSN:  1432-1351     ISO Abbreviation:  J. Comp. Physiol. A Neuroethol. Sens. Neural. Behav. Physiol.     Publication Date:  2010 Jan 
Date Detail:
Created Date:  2010-01-21     Completed Date:  2010-04-06     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101141792     Medline TA:  J Comp Physiol A Neuroethol Sens Neural Behav Physiol     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  51-9     Citation Subset:  IM    
Affiliation:
Department of Biology and Geosciences, Graduate School of Science, Osaka City University, Sumiyoshi-ku, Osaka 558-8585, Japan.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence / physiology
Animals
Cell Line
Evolution, Molecular
Eye / cytology,  metabolism*
Humans
Molecular Sequence Data
Photoreceptor Cells, Invertebrate / cytology,  metabolism*
Phylogeny
Proteomics / methods
Rhodopsin / genetics,  isolation & purification,  metabolism*
Sequence Homology, Amino Acid
Species Specificity
Spiders / cytology,  metabolism*
Vision, Ocular / physiology*
Chemical
Reg. No./Substance:
0/Rrh protein, mouse; 9009-81-8/Rhodopsin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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