title: Identification of proteolipid from an extremely halophilic archaeon Halobacterium salinarum as an N,N'-dicyclohexyl-carbodiimide binding subunit of ATP synthase.
abstract: ATP synthesis in an extremely halophilic archaeon, Halobacterium salinarum, was inhibited by N-cyclohexyl-N'-[4-(dimethylamino)-alpha-naphthyl]carbodiimide (NCD-4), a fluorescent analog of N,N'-dicyclohexylcarbodiimide (DCCD). By tracing the fluorescent signal, a hydrophobic 8-kDa protein (proteolipid) was purified from the halobacterial membrane as one of the most DCCD-reactive proteins and its N-terminal amino acid sequence was determined. The gene encoding the proteolipid was found in the region upstream of the genes encoding the two major subunits of halobacterial A-type ATPase [K. Ihara and Y.Mukohata (1991) Arch. Biochem. Biophys. 286, 111-116]. Halobacterial proteolipid was more similar in size to the proteolipid of F-type ATPase than that of V-type ATPase. However, multiple amino acid sequence alignment of proteolipids showed a higher degree of relatedness between V-type and A-type ATPase proteolipids. Together with the recent finding of a triplicate proteolipid encoding gene from the methanogenic archaeon Methanococcus jannaschii [C. J. Bult et al. (1996) Science 273, 1058-1073], proteolipids from archaea seem to have diverse characteristics in comparison with those from eubacteria or from eukaryotes.
authors.affiliation: Division of Biological Science, Graduate School of Science, Nagoya University, Japan. Kihara@bio.nagoya-u.ac.jp
authors.forename: K
authors.initials: K
authors.lastname: Ihara
authors.forename: S
authors.initials: S
authors.lastname: Watanabe
authors.forename: K
authors.initials: K
authors.lastname: Sugimura
authors.forename: I
authors.initials: I
authors.lastname: Katagiri
authors.forename: Y
authors.initials: Y
authors.lastname: Mukohata
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000235:genetics; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001483:Base Sequence; D001665:Binding Sites; D002234:Carbodiimides / Q000494:pharmacology; D004024:Dicyclohexylcarbodiimide / Q000378:metabolism*; D005057:Eukaryotic Cells / Q000201:enzymology; D019143:Evolution, Molecular; D005456:Fluorescent Dyes; D005798:Genes, Bacterial; D006217:Halobacterium / Q000737:chemistry* / Q000201:enzymology / Q000235:genetics; D008969:Molecular Sequence Data; D011387:Prokaryotic Cells / Q000201:enzymology; D011510:Proteolipids / Q000032:analysis* / Q000235:genetics; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D025262:Vacuolar Proton-Translocating ATPases
chemical_list: D001426:Bacterial Proteins; D002234:Carbodiimides; D005456:Fluorescent Dyes; D011510:Proteolipids; D004024:Dicyclohexylcarbodiimide; C038088:N-cyclohexyl-N'-(4-dimethylamino-alpha-naphthyl)carbodiimide; D000251:Adenosine Triphosphatases; D025262:Vacuolar Proton-Translocating ATPases; D006180:Proton-Translocating ATPases