Structural and functional features of yeast V-ATPase subunit C

Omri Drory, Nathan Nelson

Research output: Contribution to journalArticlepeer-review

Abstract

V-ATPase is a multi-subunit membrane protein complex, it translocates protons across biological membranes, generating electrical and pH gradients which are used for varieties of cellular processes. V-ATPase is composed of two distinct sub-complexes: a membrane bound V0 sub-complex, composed of 6 different subunits, which is responsible for proton transport and a soluble cytosolic facing V1 sub-complex, composed of 8 different subunits which hydrolyse ATP. The two sub-complexes are held together via a flexible stator. One of the main features of eukaryotic V-ATPase is its ability to reversibly dissociate to its sub-complexes in response to changing cellular conditions, which arrest both proton translocation and ATP hydrolysis, suggesting a regulation function. Subunit C (vma5p in yeast) was shown by several biochemical, genetic and recent structural data to function as a flexible stator holding the two sectors of the complex together and regulating the reversible association/dissociation of the complex, partly via association with F-actin filaments. Structural features of subunit C that allow smooth energy conversion and interaction with actin and nucleotides are discussed.

Original languageEnglish
Pages (from-to)297-303
Number of pages7
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1757
Issue number5-6
DOIs
StatePublished - May 2006

Keywords

  • 3D structure
  • Conformation
  • Mechanism
  • Subunit C
  • V-ATPase

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