Serine Protein Phosphorylation in the Non-Appressed (Stroma) Thylakoid Membranes

  • Eleonora Garcia-Véscovi
  • Héctor A. Lucero

Abstract

Thylakoid protein phosphorylation occurs in the light (1) and in the dark (E. Garcia-Vescovi and H. Lucero, unpublished). Light phosphorylation takes place mostly at threonine residues (1), is related to the state transition mechanism (2) and is catalyzed by a 64 K protein kinase (3) that is localized in the appressed thylakoid (4) where it phosphorylates LHC II (1) and some PS II core complex proteins (5). It is accepted that a single protein kinase is involved in the light phosphorylation of thylakoid proteins since the purified 64 K kinase reconstitutes in situ the light phosphorylation pattern which is inhibited by antibodies against 64 K protein (6). We have purified from thylakoid two serine protein kinases, ChlPK 1 (25 K) and ChlPK 2 (38 K) (7,8). While ChlPK 1 was predominant, ChlPK 2 contribution was substantially smaller (7). Later we observed that ChlPK 2 activity was barely detectable or even absent in some purifications (H. Lucero, unpublished) suggesting that ChlPK 2 is sensitive to the detergent extraction. Neither ChlPK 1 nor ChlPK 2 phosphorylate LHC II (8).

Keywords

Thylakoid Protein Serine Protein Protein Serine Kinase Phosphoamino Acid Analysis Core Complex Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Eleonora Garcia-Véscovi
    • 1
  • Héctor A. Lucero
    • 1
  1. 1.Area Biología, Facultad de Ciencias Bioquímicas y FarmacéuticasUniversidad Nacional de RosarioRosarioArgentina

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