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Protein tyrosine phosphorylation in the transition to light state 2 of chloroplast thylakoids

In English

Författare

  • Jens Forsberg
  • John Allen

Summary, in English

Redox dependent protein phosphorylation in chloroplast thylakoids regulates distribution of excitation energy between the two photosystems of photosynthesis, PS I and PS II. Several thylakoid phosphoproteins are known to be phosphorylated on N-terminal threonine residues exposed to the chloroplast stroma. Phosphorylation of light harvesting complex II (LHC II) on Thr-6 is thought to account for redistribution of light energy from PS II to PS I during the transition to light state 2. Here, we present evidence that a protein tyrosine kinase activity is required for the transition to light state 2. With an immunological approach using antibodies directed specifically towards either phospho-tyrosine or phospho-threonine, we observed that LHC II became phosphorylated on both tyrosine and threonine residues. The specific protein tyrosine kinase inhibitor genistein, at concentrations causing no direct effect on threonine kinase activity, was found to prevent tyrosine phosphorylation of LHC II, the transition to light state 2, and associated threonine phosphorylation of LHC II. Possible reasons for an involvement of tyrosine phosphorylation in light state transitions are proposed and discussed.

Publiceringsår

2001

Språk

Engelska

Sidor

71-79

Publikation/Tidskrift/Serie

Photosynthesis Research

Volym

68

Issue

1

Dokumenttyp

Artikel i tidskrift

Förlag

Springer

Ämne

  • Hematology

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 0166-8595