Purification and complete sequence of a small proteolipid associated with the plasma membrane H(+)-ATPase of Saccharomyces cerevisiae.
Journal of Biological ChemistryPublished 1 March 1992Open access
C Navarre, Michel Ghislain, Serge Leterme, Clotilde Ferroud, Jean‐Pierre Dufour, André Goffeau
Citations53
SJR quartileQ1
SJR score1.71
SNIP1.00
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TL;DR
NH2-terminal amino acid sequencing revealed a 38-residue polypeptide, predicted to contain an NH2- terminal transmembrane segment followed by a very basic hydrophilic domain in the purified plasma membrane H(+)-ATPase.
Abstract
The purified plasma membrane H(+)-ATPase of Schizosaccharomyces pombe and Saccharomyces cerevisiae display, in addition to the catalytic subunit of 100 kDa, a highly mobile component, soluble in chloroform/methanol. Chloroform/methanol extraction of S. cerevisiae plasma membranes led to isolation of a low molecular weight proteolipid identical to that present in purified H(+)-ATPase. NH2-terminal amino acid sequencing revealed a 38-residue polypeptide with a calculated molecular mass of 4250 Da. The polypeptide lacks the first two NH2-terminal amino acids as compared with the deduced sequence of the PMP1 gene (for plasma membrane proteolipid) isolated by hybridization with an oligonucleotide probe corresponding to an internal amino acid sequence of the proteolipid. The polypeptide is predicted to contain an NH2-terminal transmembrane segment followed by a very basic hydrophilic domain.
Keywords
Biochemistry, Genetics and Molecular Biology
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