The stabilizing residues and the functional domains in the hyperthermophilic V-ATPase of Desulfurococcus

Biochemical and Biophysical Research Communications
H ShibuiY Kagawa

Abstract

To clarify a universal mechanism of the intramolecular rotation of ATP-synthase, an operon encoding a stable, ancestral ATPase was cloned from a heterotrophic archaeum Desulfurococcus strain SY. The operon of about 7 kbp contained genes E, C, G, A, B and D encoding subunits with predicted molecular weights of 23,217, 41,659, 11,499, 65,476, 52,295, and 24,897, respectively. The sequence was compared with that of Na-ATPase of Enterococcus hirae, A-ATPase of Halobacterium salinarium, V-ATPase of Methanosarcina mazei, and ATP synthase of Methanococcus jannaschii, which are homologous. (1) The cause of hyperthermostability: The main exchanges in the amino acid residues of hyperthermophilic proteins included Asp --> Glu (11 residues of A subunit of E.h.) and, Ser --> Ala. (2) The domains needed for the intramolecular rotation: The domains similar to those established in F-type ATPases were also found in the V-type ATPases of species with a different energy metabolism.

Citations

Nov 26, 2002·Molecular Biology and Evolution·J Peter GogartenJeffrey G Lawrence
Dec 21, 2006·Genetics·Samuel LiégeoisMichel Labouesse
Dec 6, 1997·Biochemical and Biophysical Research Communications·Y Kagawa, T Hamamoto
Aug 27, 1999·Advances in Biophysics·Y Kagawa
Sep 8, 1999·Microbiology and Molecular Biology Reviews : MMBR·G SchäferV Müller

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