Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1988 Dec;170(12):5960–5962. doi: 10.1128/jb.170.12.5960-5962.1988

Isolation of subunits from Methanosarcina barkeri ATPase: nucleotide-binding site in the alpha subunit.

K Inatomi 1, M Maeda 1
PMCID: PMC211715  PMID: 2973460

Abstract

The alpha (62,000-dalton) and beta (49,000-dalton) subunits of Methanosarcina barkeri ATPase were purified to homogeneity. The subunits and ATPase complex were trypsinized in the presence of various nucleotides. ATP and ADP changed the trypsin sensitivity of the alpha subunit in the complex and isolated forms, suggesting the presence of a nucleotide-binding site in the alpha subunit.

Full text

PDF
5960

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Denda K., Konishi J., Oshima T., Date T., Yoshida M. The membrane-associated ATPase from Sulfolobus acidocaldarius is distantly related to F1-ATPase as assessed from the primary structure of its alpha-subunit. J Biol Chem. 1988 May 5;263(13):6012–6015. [PubMed] [Google Scholar]
  2. Doddema H. J., Hutten T. J., van der Drift C., Vogels G. D. ATP hydrolysis and synthesis by the membrane-bound ATP synthetase complex of Methanobacterium thermoautotrophicum. J Bacteriol. 1978 Oct;136(1):19–23. doi: 10.1128/jb.136.1.19-23.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Futai M., Kanazawa H. Structure and function of proton-translocating adenosine triphosphatase (F0F1): biochemical and molecular biological approaches. Microbiol Rev. 1983 Sep;47(3):285–312. doi: 10.1128/mr.47.3.285-312.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hippe H., Caspari D., Fiebig K., Gottschalk G. Utilization of trimethylamine and other N-methyl compounds for growth and methane formation by Methanosarcina barkeri. Proc Natl Acad Sci U S A. 1979 Jan;76(1):494–498. doi: 10.1073/pnas.76.1.494. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hsu S. Y., Noumi T., Takeyama M., Maeda M., Ishibashi S., Futai M. Beta-subunit of Escherichia coli F1-ATPase. An amino acid replacement within a conserved sequence (G-X-X-X-X-G-K-T/S) of nucleotide-binding proteins. FEBS Lett. 1987 Jun 29;218(2):222–226. doi: 10.1016/0014-5793(87)81050-5. [DOI] [PubMed] [Google Scholar]
  6. Inatomi K. Characterization and purification of the membrane-bound ATPase of the archaebacterium Methanosarcina barkeri. J Bacteriol. 1986 Sep;167(3):837–841. doi: 10.1128/jb.167.3.837-841.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Konishi J., Wakagi T., Oshima T., Yoshida M. Purification and properties of the ATPase solubilized from membranes of an acidothermophilic archaebacterium, Sulfolobus acidocaldarius. J Biochem. 1987 Dec;102(6):1379–1387. doi: 10.1093/oxfordjournals.jbchem.a122184. [DOI] [PubMed] [Google Scholar]
  8. Kristjansson H., Sadler M. H., Hochstein L. I. Halobacterial adenosine triphosphatases and the adenosine triphosphatase from Halobacterium saccharovorum. FEMS Microbiol Rev. 1986;39:151–157. doi: 10.1016/0378-1097(86)90074-1. [DOI] [PubMed] [Google Scholar]
  9. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  10. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  11. Lübben M., Schäfer G. A plasma-membrane associated ATPase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. Eur J Biochem. 1987 May 4;164(3):533–540. doi: 10.1111/j.1432-1033.1987.tb11159.x. [DOI] [PubMed] [Google Scholar]
  12. Mountfort D. O. Evidence from ATP synthesis driven by a proton gradient in Methanosarcina barkeri. Biochem Biophys Res Commun. 1978 Dec 29;85(4):1346–1351. doi: 10.1016/0006-291x(78)91151-8. [DOI] [PubMed] [Google Scholar]
  13. Nanba T., Mukohata Y. A membrane-bound ATPase from Halobacterium halobium: purification and characterization. J Biochem. 1987 Sep;102(3):591–598. doi: 10.1093/oxfordjournals.jbchem.a122092. [DOI] [PubMed] [Google Scholar]
  14. Senda M., Kanazawa H., Tsuchiya T., Futai M. Conformational change of the alpha subunit of Escherichia coli F1 ATPase: ATP changes the trypsin sensitivity of the subunit. Arch Biochem Biophys. 1983 Feb 1;220(2):398–404. doi: 10.1016/0003-9861(83)90429-0. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES