Abstract
Extreme halophiles newly collected from Argentine salt flats were characterized, in one of which, Haloarcula (sp. arg-1), light-driven retinal protein ion pumps were found. The proton pump, cruxrhodopsin-1, shows amino acid sequence homologies of 52% to bacteriorhodopsin and 48% to archaerhodopsin-1. The anion pump, cruxhalorhodopsin-1, identified partially as a 394bp polymerase chain reaction product, shows homologies of 70% to halorhodopsin, and 72% to pharaonis halorhodopsin. The ion pumps (and possibly sensors still to be found) in Haloarcula sp. arg-1, which constitute the cruxrhodopsin-1 family, are distinct from the bacteriorhodopsin and the archaerhodopsin families/tribes.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Archaeal Proteins*
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Bacterial Proteins / classification
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Bacterial Proteins / genetics
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Bacterial Proteins / physiology
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Bacteriorhodopsins / classification
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Bacteriorhodopsins / genetics
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Base Sequence
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Cloning, Molecular
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Genes, Bacterial / genetics*
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Halobacteriaceae / genetics*
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Ion Pumps / genetics*
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Ion Pumps / physiology
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Ion Pumps / radiation effects
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Light
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Membranes / metabolism
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Molecular Sequence Data
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Retinal Pigments / classification
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Retinal Pigments / genetics
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Retinal Pigments / physiology
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Rhodopsin / chemistry
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Rhodopsin / genetics*
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Sequence Analysis, DNA
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Sequence Homology, Amino Acid
Substances
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Archaeal Proteins
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Bacterial Proteins
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Ion Pumps
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Retinal Pigments
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archaerhodopsin protein, Archaea
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Bacteriorhodopsins
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Rhodopsin
Associated data
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GENBANK/S74069
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GENBANK/S74070