Acetylation and phosphorylation control both local and global stability of the chloroplast F₁ ATP synthase.

ABSTRACT: ATP synthases (ATPases) are enzymes that produce ATP and control the pH in the cell or cellular compartments. While highly conserved over different species, ATPases are structurally well-characterised but the existence and functional significance of many post-translational modifications (PTMs) is not well understood. We combined a range of mass spectrometric techniques to unravel the location and extent of PTMs in the chloroplast ATP synthase (cATPase) purified from spinach leaves. We identified multiple phosphorylation and acetylation sites and found that both modifications stabilise binding of ε and δ subunits. Comparing cross-linking of naturally modified cATPase with the in vitro deacetylated enzyme revealed a major conformational change in the ε subunit in accord with extended and fol

SUBMITTER: Schmidt C 

PROVIDER: S-EPMC5343439 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature