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Temperature‐dependent hyper‐activation of monoglucosyldiacylglycerol synthase is post‐translationally regulated in Synechocystis sp. PCC 6803
Author(s) -
Shimojima Mie,
Tsuchiya Mami,
Ohta Hiroyuki
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.06.033
Subject(s) - synechocystis , chemistry , enzyme , biochemistry , atp synthase , recombinant dna , covalent bond , phosphorylation , mutant , gene , organic chemistry
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.