The carboxyl-terminal processing of precursor D1 protein of the photosystem II reaction center

Kimiyuki Satoh, Yumiko Yamamoto

Research output: Contribution to journalReview article

26 Citations (Scopus)

Abstract

The D1 protein, a key subunit of photosystem II reaction center, is synthesized as a precursor form with a carboxyl-terminal extension, in oxygenic photosynthetic organisms with some exceptions. This part of the protein is removed by the action of an endopeptidase, and the proteolytic processing is indispensable for the manifestation of oxygen-evolving activity in photosynthesis. The carboxyl-terminus of mature D1 protein, which appears upon the cleavage, has recently been demonstrated to be a ligand for a manganese atom in the Mn4Ca-cluster, which is responsible for the water oxidation chemistry in photosystem II, based on the isotope-edited Fourier transform infrared spectroscopy and the X-ray crystallography. On the other hand, the structure of a peptidase involved in the cleavage of precursor D1 protein has been resolved at a higher resolution, and the enzyme-substrate interactions have extensively been analyzed both in vivo and in vitro. The present article briefly summarizes the history of research and the present state of our knowledge on the carboxyl-terminal processing of precursor D1 protein in the photosystem II reaction center.

Original languageEnglish
Pages (from-to)203-215
Number of pages13
JournalPhotosynthesis research
Volume94
Issue number2-3
DOIs
Publication statusPublished - Nov 2007

Keywords

  • Carboxyl-terminal processing
  • CtpA
  • D1 protein
  • MnCa-cluster
  • Oxygen evolution
  • Photosystem II
  • Precursor D1 protein
  • Processing protease
  • psbA gene

ASJC Scopus subject areas

  • Biochemistry
  • Plant Science
  • Cell Biology

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