Amino acid sequence of the alpha and beta subunits of Methanosarcina barkeri ATPase deduced from cloned genes. Similarity to subunits of eukaryotic vacuolar and F0F1-ATPases

• Published in: The Journal of biological chemistry Vol. 264; no. 19; pp. 10954 - 10959
• Main Authors: KEN-ICHI INATOMI, SEIJI EYA, MAEDA, M, FUTAI, M
• Format: Journal Article
• Language: English
• Published: Bethesda, MD American Society for Biochemistry and Molecular Biology 05.07.1989
• Subjects: Adenosine Triphosphatases - genetics; Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Base Sequence; Biological and medical sciences; Cloning, Molecular; Enzymes and enzyme inhibitors; Escherichia coli - enzymology; Euryarchaeota - enzymology; Euryarchaeota - genetics; Fundamental and applied biological sciences. Psychology; Genes, Bacterial; Gram-Negative Chemolithotrophic Bacteria - enzymology; Hydrolases; Molecular Sequence Data; Neurospora crassa - enzymology; Oxidative Phosphorylation Coupling Factors; Plants - enzymology; Proton-Translocating ATPases; Saccharomyces cerevisiae - enzymology; Sequence Homology, Nucleic Acid; Vacuoles - enzymology; Methanomicrobiales; Molecular hybridization; Eucaryote; Methanosarcina barkeri; Nucleotide sequence; Archaeobacteria; ATPase; Bacteria; Methanosarcinaceae; Homology; Molecular cloning; Subunit
• ISSN: 0021-9258; 1083-351X

The atpA and atpB genes coding for the alpha and beta subunits, respectively, of membrane ATPase were cloned from a methanogen Methanosarcina barkeri, and the amino acid sequences of the two subunits were deduced from the nucleotide sequences. The methanogenic alpha (578 amino acid residues) and beta (459 amino acid residues) subunits were highly homologous to the large and small subunits, respectively, of vacuolar H+-ATPases; 52% of the residues of the methanogenic alpha subunit were identical with those of the large subunit of vacuolar enzyme of carrot or Neurospora crassa, respectively, and 59, 60, and 59% of the residues of the methanogenic beta subunit were identical with those of the small subunits of N. crassa, Arabidopsis thaliana, and Sacharomyces cerevisiae, respectively. The methanogenic subunits were also highly homologous to the corresponding subunits of Sulfolobus acidocaldarius ATPase. The methanogenic alpha and beta subunits showed 22 and 24% identities with the beta and the alpha subunits of Escherichia coli F1, respectively. Furthermore, important amino acid residues identified genetically in the E. coli enzyme were conserved in the methanogenic enzyme. This sequence conservation suggests that vacuolar, F1, methanogenic, and S. acidocaldarius ATPases were derived from a common ancestral enzyme.