4.5 Article

Dephosphorylation of photosystem II proteins and phosphorylation of CP29 in barley photosynthetic membranes as a response to water stress

Journal

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1787, Issue 10, Pages 1238-1245

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2009.04.012

Keywords

Dephosphorylation; Lateral migration; Phosphorylation; Photosystem II; Thylakoid phosphatase

Funding

  1. National Key Basic Research '973' Program of China [2009CB118500]
  2. National Nature Science Foundation of China [30670166, 30800071]
  3. New Century Excellent Talents Program [NCET-05-0786]

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Kinetic studies of protein dephosphorylation in barley thylakoid membranes revealed accelerated dephosphorylation of photosystem 11 (PSII) proteins, and meanwhile rapidly induced phosphorylation of a light-harvesting complex (LHCII) b4, CP29 under water stress. Inhibition of dephosphorylation aggravates stress damages and hampers photosystem recovery after rewatering. This increased dephosphorylation is catalyzed by both intrinsic and extrinsic membrane protein phosphatase. Water stress did not cause any thylakoid destacking, and the lateral migration from granum membranes to stroma-exposed lamellae was only found to CP29, but not other PSII proteins. Activation of plastid proteases and release of TLP40, an inhibitor of the membrane phosphatases, were also enhanced during water stress. Phosphorylation of CP29 may facilitate disassociation of LHCII from PSII complex, disassembly of the LHCII trimer and its subsequent degradation, while general dephosphorylation of PSII proteins may be involved in repair cycle of PSII proteins and stress-response-signaling. (C) 2009 Elsevier B.V. All rights reserved.

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