Epitope-tagged constructs of the yeast plasma-membrane H(+)-ATPase.

Abstract:

:In this study, two different epitope tags (HA, c-myc) were introduced near the N terminus of the yeast PMA1 H(+)-ATPase. The resulting proteins were indistinguishable from the wild-type ATPase in their ability to travel through the secretory pathway, as judged by quantitative immunoblotting of isolated secretory vesicles. Furthermore, there were no significant abnormalities in ATPase activity (including K(m) for MgATP, Vmax, pH optimum, and IC50 for inhibition by vanadate) or in ATP-dependent proton pumping. Finally, the epitope-tagged ATPases could support normal growth and displayed the expected activation by glucose.

journal_name

IUBMB Life

journal_title

IUBMB life

authors

dos Santos CF,DeWitt ND,Gupta SS,Allen KE,Slayman CW

doi

10.1080/15216540050022494

keywords:

subject

Has Abstract

pub_date

2000-02-01 00:00:00

pages

153-9

issue

2

eissn

1521-6543

issn

1521-6551

journal_volume

49

pub_type

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