The ATP binding site of the yeast plasma membrane proton-translocating ATPase.
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چکیده
منابع مشابه
Topology of the yeast plasma membrane proton-translocating ATPase.
Four proteases have been used to assess the topology of the H+-ATPase from Saccharomyces cerevisiae reconstituted into phosphatidylserine vesicles. Limited proteolysis by trypsin and alpha-chymotrypsin inactivates the enzyme and produces stable, membrane-bound fragments. Sequence analyses of these peptides have located the peptide bonds hydrolyzed. The labile bonds are on opposite sides of a ce...
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The yeast vacuolar proton-translocating ATPase (VATPase) is structurally very similar to the V-ATPases of other fungi, plants and animals (for reviews, see Stevens and Forgac, 1997; Forgac, 1999; Nelson and Harvey, 1999). In all these systems, the V-ATPase is composed of a complex of peripheral membrane proteins containing the ATP binding sites attached to a complex of integral membrane protein...
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Michel Ronjat, Jean Jacques Lacapere$, Jean-Pierre Dufourp, and Yves Dupont From the Luboratoire de Bwphysique Mol=Gculaire et Cellulaire, Centre d’Etudes Nuckaires de Grenoble, 3804l-Grenoble, France, the $Service de Biophysique, Departement de Biologic, Centre d’Etudes Nuckaires de Saclay, 91190-Gif-sur-Yuette, France, and the ILabOratoire des Sciences et Technologies Brassicoles, Uniuersite ...
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For Ca(2+) to function as a second messenger in signal transduction, it is essential that plant cells maintain low cytoplasmic Ca(2+) levels relative to internal organelles and the apoplast. At the plasma membrane, Ca(2+) is actively transported out of the cytoplasm and current evidence supports the involvement of a primary Ca(2+)-translocating ATPase in mediating this energy-dependent process....
متن کاملMembrane topography of the coupling ion binding site in Na+-translocating F1F0 ATP synthase.
A carbodiimide with a photoactivatable diazirine substituent was synthesized and incubated with the Na(+)-translocating F(1)F(0) ATP synthase from both Propionigenium modestum and Ilyobacter tartaricus. This caused severe inhibition of ATP hydrolysis activity in the absence of Na(+) ions but not in its presence, indicating the specific reaction with the Na(+) binding c-Glu(65) residue. Photocro...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1990
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)40013-6