Effect of divalent cations on the ATPase activity of Escherichia coli SecA

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It was found that Ca2+ stimulates the intrinsic SecA ATPase activity in the absence as well as in the presence of liposome, On the other hand, Mg2+, the general cofactor for ATPase. did not affect the intrinsic SecA ATPase but reduced the portion of ATPase activity enhanced by. Ca2+. The enhancement of SecA ATPase activity correlated well with the increase in 8-anilino-1-naphthalene-sulfonic acid binding of SecA, suggesting that increased exposure of hydrophobic residues stimulates the enzyme activity. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
Publisher
ELSEVIER SCIENCE BV
Issue Date
2001-03
Language
English
Article Type
Article
Keywords

RIBOSE-BINDING-PROTEIN; MODEL MEMBRANES; LIPID BILAYER; PHOSPHOLIPIDS; TRANSLOCATION; PENETRATION; MECHANISMS; VESICLES; TERMINUS; DOMAINS

Citation

FEBS LETTERS, v.493, no.1, pp.12 - 16

ISSN
0014-5793
URI
http://hdl.handle.net/10203/78827
Appears in Collection
BS-Journal Papers(저널논문)
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