title: Defined subcomplexes of the A1 ATPase from the archaeon Methanosarcina mazei Gö1: biochemical properties and redox regulation.
abstract: The potential A(1) ATPase genes ahaA, ahaB, ahaC, ahaD, ahaE, ahaF, and ahaG from the anaerobic archaeon Methanosarcina mazei Gö1 were overexpressed in Escherichia coli DK8 (pTL2). An A(1) complex was purified to apparent homogeneity and shown by Western blot and N-terminal sequence analyses to contain subunits A, B, C, D, and F but to be devoid of subunits E and G. Further removal of subunit C was without effect on ATPase activity. The enzyme was most active at pH 5.2 and required bisulfite and acetate for maximal activity. Kinetic studies confirmed three new inhibitors for A(1) ATPases (diethylstilbestrol and its derivatives hexestrol and dienestrol) and identified redox modulation as a new type of regulation of archaeal A(1) ATPases.
authors.affiliation: Section Microbiology, Department Biology I, Ludwig-Maximilians-University, Maria-Ward-Str. 1a, D-80638 Munich, Germany.
authors.forename: Thorsten
authors.initials: T
authors.lastname: Lemker
authors.forename: Gerhard
authors.initials: G
authors.lastname: Grüber
authors.forename: Roland
authors.initials: R
authors.lastname: Schmid
authors.forename: Volker
authors.initials: V
authors.lastname: Müller
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D019843:Archaeal Proteins; D015153:Blotting, Western; D004305:Dose-Response Relationship, Drug; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D017020:Methanosarcina / Q000201:enzymology*; D008958:Models, Molecular; D010084:Oxidation-Reduction; D010957:Plasmids / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D006180:Proton-Translocating ATPases / Q000737:chemistry*
chemical_list: D019843:Archaeal Proteins; C113203:A1A0 ATPase, Methanosarcina mazei; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases