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Isolation and Mapping of a Putative b Subunit of Human ATP Synthase (ATP-BL) from Human Leukocytes
Author(s) -
Jun Sugimoto
Publication year - 1999
Publication title -
dna research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.647
H-Index - 98
eISSN - 1756-1663
pISSN - 1340-2838
DOI - 10.1093/dnares/6.1.29
Subject(s) - biology , complementary dna , atp synthase , atp synthase gamma subunit , microbiology and biotechnology , protein subunit , homology (biology) , open reading frame , peptide sequence , v atpase , biochemistry , atpase , nucleic acid sequence , amino acid , gene , enzyme , atp hydrolysis
From a human-leukocyte cDNA library, we cloned cDNA encoding a novel protein, which has a significant homology with the b subunit of ATP synthase (proton-transporting ATPase, F1F0-ATPase; EC3.6.1.34) derived from Anabaena sp. strain PCC 7120. The cDNA has an open reading frame of 1314 nucleotides corresponding to 438 amino acids. The coding sequence was 37.9% identical over 57 amino acid with b subunit of ATP synthase. The 34-amino-acid region of the predicted peptide sequence displays a coiled-coil motif that could form a complex with some other protein(s). We designated this novel gene as ATP-BL because of its homology to the b subunit of ATP synthase. The ATP-BL locus was mapped by fluorescence in situ hybridization (FISH) and radiation hybrid mapping to the q24 region of chromosome 16.

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