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

Abstract:

: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.

journal_name

Photosynth Res

journal_title

Photosynthesis research

authors

Forsberg J,Allen JF

doi

10.1023/A:1011891017067

subject

Has Abstract

pub_date

2001-01-01 00:00:00

pages

71-9

issue

1

eissn

0166-8595

issn

1573-5079

journal_volume

68

pub_type

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