Temperature-dependent hyper-activation of monoglucosyldiacylglycerol synthase is post-translationally regulated in Synechocystis sp. PCC 6803

FEBS Lett. 2009 Jul 21;583(14):2372-6. doi: 10.1016/j.febslet.2009.06.033. Epub 2009 Jun 21.

Abstract

The mechanism of monoglucosyldiacylglycerol (MGlcDG) increase following heat shock in Synechocystis sp. PCC 6803 was examined by measuring MGlcDG synthase (Sll1377) activity. Temperature-dependent activation of Sll1377 was observed in the membrane fraction of Synechocystis sp. PCC 6803, whereas the Sll1377 protein level remained unchanged, suggesting that the activity is post-translationally regulated without covalent modification of Sll1377 by soluble enzymes. Four individual mutations introduced into recombinant Sll1377 (D147, D200, R329, and R331) significantly reduced the activity and blocked temperature-dependent activation, suggesting that these amino acid residues are essential for Sll1377 activity at both normal growth temperature and the higher temperature.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins* / genetics
  • Bacterial Proteins* / metabolism
  • Cell Membrane / enzymology
  • Enzyme Activation*
  • Gene Expression Regulation, Bacterial*
  • Gene Expression Regulation, Enzymologic*
  • Glucosyltransferases* / genetics
  • Glucosyltransferases* / metabolism
  • Glycolipids / metabolism
  • Hot Temperature
  • Mutation
  • Protein Processing, Post-Translational*
  • Synechocystis* / enzymology
  • Synechocystis* / genetics

Substances

  • Bacterial Proteins
  • Glycolipids
  • glucosyl diacylglycerol
  • Glucosyltransferases
  • 1,2-diacylglycerol 3-glucosyltransferase