Temperature-dependent hyper-activation of monoglucosyldiacylglycerol synthase is post-translationally regulated in Synechocystis sp. PCC 6803
In: FEBS Letters, Jg. 583 (2009-07-21), Heft 14, S. 2372-2376
Online
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Zugriff:
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. [Copyright &y& Elsevier]
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Temperature-dependent hyper-activation of monoglucosyldiacylglycerol synthase is post-translationally regulated in Synechocystis sp. PCC 6803
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Autor/in / Beteiligte Person: | Shimojima, Mie ; Tsuchiya, Mami ; Ohta, Hiroyuki |
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Zeitschrift: | FEBS Letters, Jg. 583 (2009-07-21), Heft 14, S. 2372-2376 |
Veröffentlichung: | 2009 |
Medientyp: | academicJournal |
ISSN: | 0014-5793 (print) |
DOI: | 10.1016/j.febslet.2009.06.033 |
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