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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Guerra, Guadalupe Miranda, Manuel Allen, Kenneth E. Pardo, Juan Pablo Slayman, Carolyn W. Petrov, Valery V. |
| Description | Author Affiliation: Guerra G ( Departmento de Microbiologia, Escuela Nacional de Ciencias Biologicas, I.P.N., Mexico, D.F., Mexico.) |
| Abstract | Of the four transmembrane helices (M4, M5, M6, and M8) that pack together to form the ion-binding sites of P(2)-type ATPases, M8 has until now received the least attention. The present study has used alanine-scanning mutagenesis to map structure-function relationships throughout M8 of the yeast plasma-membrane H(+)-ATPase. Mutant forms of the ATPase were expressed in secretory vesicles and at the plasma membrane for measurements of ATP hydrolysis and ATP-dependent H(+) pumping. In secretory vesicles, Ala substitutions at a cluster of four positions near the extracytoplasmic end of M8 led to partial uncoupling of H(+) transport from ATP hydrolysis, while substitution of Ser-800 (close to the middle of M8) by Ala increased the apparent stoichiometry of H(+) transport. A similar increase has previously been reported following the substitution of Glu-803 by Gln (Petrov, V. et al., J. Biol. Chem. 275:15709-15718, 2000) at a position known to contribute directly to Ca(2+) binding in the Ca(2+)-ATPase of sarcoplasmic reticulum (Toyoshima, C., et al., Nature 405: 647-655, 2000). Four other mutations in M8 interfered with H(+)-ATPase folding and trafficking to the plasma membrane; based on homology modeling, they occupy positions that appear important for the proper bundling of M8 with M5, M6, M7, and M10. Taken together, these results point to a key role for M8 in the biogenesis, stability, and physiological functioning of the H(+)-ATPase. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 10 |
| Volume Number | 1768 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2007-10-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Cell Membrane Enzymology Proton-Translocating ATPases Chemistry Saccharomyces Cerevisiae Proteins Saccharomyces Cerevisiae Amino Acid Sequence Hydrogen-Ion Concentration Molecular Sequence Data Physiology Structure-Activity Relationship Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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