Open AccessATP4 , the structural gene for yeast F 0 F 1 ATPase subunit 4
Author(s) -
VELOURS Jean,
DURRENS Pascal,
AIGLE Michel,
GUÉRIN Bernard
Publication year - 1988
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1988.tb13745.x
Subject(s) - protein subunit , biology , specificity factor , nucleic acid sequence , peptide sequence , gene , saccharomyces cerevisiae , biochemistry , scn3a , open reading frame , structural gene , oligonucleotide , microbiology and biotechnology , escherichia coli , plasmid , homology (biology) , amino acid , g alpha subunit , rna polymerase
A plasmid containing the gene coding for the Saccharomyces cerevisiae F 0 F l ATPase subunit 4 was isolated from a yeast genomic DNA library using the oligonucleotide probe procedure. The gene and the surrounding regions were cloned into M13 tg 130 and M13 tg 131 phage vectors. A 732‐base‐pair open reading frame encoding a 244‐amino‐acid polypeptide is described. The nucleotide sequence predicts that subunit 4 is probably derived from a precursor protein with a hydrophilic and basic 35‐amino‐acid leader sequence. Mature subunit 4 contains 209 amino acid residues and the predicted molecular mass is 23250 Da. This subunit presents amphiphilic behaviour with two distinct domains. A high α‐helix content of 77% was predicted from the sequence. Subunit 4 shows homology with the b subunit of Escherichia coli ATP synthase.