Involvement of a Chloroplast HSP70 Heat Shock Protein in the Integration of a Protein (Light-Harvesting Complex Protien Precursor) into the Thylakoid Membrane

Molecular chaperones, including those belonging to the 70-kDa family of heat shock proteins (HSP70), assist both the translocation of proteins across membranes and their assembly into oligomeric complexes. We purified a chloroplast HSP70 (ct-HSP70) and demonstrated that it plays a major role in the ... Ausführliche Beschreibung

1. Person: Yalovsky, Shaul
Weitere Personen: Paulsen, Harald verfasserin; Michaeli, Dorit verfasserin; Chitnis, Parag R. verfasserin; Nechushtai, Rachel verfasserin
Quelle: in Proceedings of the National Academy of Sciences of the United States of America Vol. 89, No. 12 (1992), p. 5616-5619
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Format: Online-Artikel
Sprache: English
Veröffentlicht: 1992
Beschreibung: Online-Ressource
Schlagworte: research-article
Biophysics
Chaperone
Membrane Integration
Biogenesis
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Anmerkung: Copyright: Copyright 1992 The National Academy of Sciences of the United States of America
Zusammenfassung: Molecular chaperones, including those belonging to the 70-kDa family of heat shock proteins (HSP70), assist both the translocation of proteins across membranes and their assembly into oligomeric complexes. We purified a chloroplast HSP70 (ct-HSP70) and demonstrated that it plays a major role in the insertion of the precursor of the major light-harvesting complex of photosystem II (pLHCP; an integral membrane protein) into the thylakoids (the inner membranes of the chloroplast). Addition of the purified ct-HSP70 is necessary for efficient insertion of pLHCP into isolated thylakoid membranes. This activity of the purified ct-HSP70 is similar to that previously reported for the total stromal extract. When the chloroplast stromal extract is depleted of HSP70, a correlative reduction in the insertion activity of pLHCP is observed. The interaction between the ct-HSP70 and pLHCP involves physical association. The purified HSP70 acts directly on the membrane protein, presumably prevents its refolding, and thereby helps to maintain its competence for insertion into membranes.
ISSN: 0027-8424

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