The 9-kDa phosphoprotein of photosystem II. Generation and characterisation of Chlamydomonas mutants lacking PSII-H and a site-directed mutant lacking the phosphorylation site

Helen E. O'Connor, Stuart V. Ruffle, Amanda J. Cain, Zsuzsanna Deak, Imre Vass, Jonathan H.A. Nugent, Saul Purton

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

The chloroplast gene psbH encodes a 9-10 kDa thylakoid membrane protein (PSII-H) that is associated with photosystem II and is subject to light- dependent phosphorylation at a threonine residue located on the stromal side of the membrane. The function of PSII-H is not known, neither is it clear what regulatory role phosphorylation may play in the control of PSII activity. Using particle gun-mediated transformation, we have created chloroplast transformants of Chlamydomonas reinhardtii in which the synthesis of PSII-H is prevented by the disruption of psbH, or in which the phosphorylatable threonine is replaced by alanine through site-directed mutagenesis of the gene. The mutants lacking PSII-H have a photosystem II- deficient phenotype, with no detectable functioning PSII complex present in whole cells or isolated thylakoid membranes. In contrast, the alanine mutant (T3A) grows photoautotrophically, and PSII activity is comparable to wild- type cells as determined by various biochemical and biophysical assays.

Original languageEnglish
Pages (from-to)63-72
Number of pages10
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1364
Issue number1
DOIs
Publication statusPublished - Apr 14 1998

Keywords

  • (Chlamydomonas)
  • Mutagenesis
  • PSII-H
  • Phosphoprotein
  • Photosystem II
  • psbH

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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