Membrane protein damage and repair: removal and replacement of inactivated 32-kilodalton polypeptides in chloroplast membranes.

I. Ohad, D. J. Kyle, C. J. Arntzen

Research output: Contribution to journalArticle

338 Citations (Scopus)

Abstract

Incubation of Chlamydomonas reinhardii cells at light levels that are several times more intense than those at which the cells were grown results in a loss of photosystem II function (termed photoinhibition). The loss of activity corresponded to the disappearance from the chloroplast membranes of a lysine-deficient, herbicide-binding protein of 32,000 daltons which is thought to be the apoprotein of the secondary quinone electron acceptor of photosystem II (the QB protein). In vivo recovery from the damage only occurred following de novo synthesis (replacement) of the chloroplast-encoded QB protein. We believe that the turnover of this protein is a normal consequence of its enzymatic function in vivo and is a physiological process that is necessary to maintain the photosynthetic integrity of the thylakoid membrane. Photoinhibition occurs when the rate of inactivation and subsequent removal exceeds the rate of resynthesis of the QB protein.

Original languageEnglish (US)
Pages (from-to)481-485
Number of pages5
JournalJournal of Cell Biology
Volume99
Issue number2
StatePublished - Aug 1984
Externally publishedYes

Fingerprint

Chloroplasts
Membrane Proteins
Photosystem II Protein Complex
Peptides
Membranes
Physiological Phenomena
Chloroplast Proteins
Chlamydomonas reinhardtii
Thylakoids
Proteins
Apoproteins
Herbicides
Lysine
Carrier Proteins
Electrons
Light

ASJC Scopus subject areas

  • Cell Biology

Cite this

Membrane protein damage and repair : removal and replacement of inactivated 32-kilodalton polypeptides in chloroplast membranes. / Ohad, I.; Kyle, D. J.; Arntzen, C. J.

In: Journal of Cell Biology, Vol. 99, No. 2, 08.1984, p. 481-485.

Research output: Contribution to journalArticle

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