Glu-44 in the amino-terminal α-Helix of yeast vacuolar atpase e subunit (Vma4p) has a role for VoV1 assembly

10Citations
Citations of this article
24Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

Background: The V-ATPase is inactivated by reversible disassembly upon glucose starvation. Results: Glu-44 of the V-ATPase E subunit was identified by alanine scanning mutagenesis with reduced disassembly under glucose starvation. Conclusion: Mutations to Glu-44 of the E subunit disrupt normal disassembly of the V-ATPase and affect catalytic activity. Significance: Interactions with the E subunit in the V-ATPase are important for controlling disassembly and catalytic activity. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc. Published in the U.S.A.

Cite

CITATION STYLE

APA

Okamoto-Terry, H., Umeki, K., Nakanishi-Matsui, M., & Futai, M. (2013). Glu-44 in the amino-terminal α-Helix of yeast vacuolar atpase e subunit (Vma4p) has a role for VoV1 assembly. Journal of Biological Chemistry, 288(51), 36236–36243. https://doi.org/10.1074/jbc.M113.506741

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free