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Characterization of Mutants with Alterations of the Phosphorylation Site in the D2 Photosystem II Polypeptide of Chlamydomonas reinhardtii1

Mark M. Fleischmann and Jean-David Rochaix*

Departments of Molecular Biology and Plant Biology, University of Geneva, 1211 Geneva 4, Switzerland

We have changed the potential phosphorylation site, a threonine residue at position 2 of the D2 polypeptide of the photosystem II complex of Chlamydomonas reinhardtii, to alanine, valine, aspartate, proline, glycine, or glutamate. Mutants with neutral amino acid changes did not display any phenotype with regard to photoautotrophic growth, light sensitivity, fluorescence transients, or photoinhibition. Pulse labeling of these mutants with 32P indicated that a phosphorylated protein of the same size as D2 is absent in these mutants, suggesting that threonine-2 is indeed the unique phosphorylation site of D2. In contrast, mutants in which threonine-2 has been replaced with acidic residues are deficient in photosystem II. Use of chimeric genes containing the psbD 5'-untranslated region revealed that the initiation of translation was not affected in these mutants, but the mutations interfered with a later step of D2 synthesis and accumulation.

1   This work was supported by grant no. 3100-050895.97 from the Swiss National Science Foundation.
*   Corresponding author; e-mail jean-david.rochaix{at}molbio.unige.ch; fax 41-22-702-68-68.

Plant Physiol. (1999) 119: 1557-1566
Copyright Clearance Center:   0032-0889/99/119//10
© 1999 American Society of Plant Physiologists




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