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Lumenal exposed regions of the D1 protein of PSII are long enough to be degraded by the chloroplast Deg1 protease.
Knopf, Ronit Rimon; Adam, Zach.
Afiliación
  • Knopf RR; The Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, Faculty of Agriculture, Food and Environment, The Hebrew University of Jerusalem, Rehovot, 76100, Israel.
  • Adam Z; Evogene Ltd., Rehovot, 76120, Israel.
Sci Rep ; 8(1): 5230, 2018 03 27.
Article en En | MEDLINE | ID: mdl-29588501
ABSTRACT
Degradation of the D1 protein of photosystem II (PSII) reaction center is a pre-requisite for the repair cycle from photoinhibition. Two types of thylakoid proteases, FtsH and Deg, have been demonstrated to participate in this process. However, the location of the proteolytic sites of the lumenal Deg1 protease within its internal sphere raised the question whether the lumenal-exposed regions of D1 are indeed long enough to reach these sites. Implanting these regions into the stable GFP rendered it sensitive to the presence of Deg1 in vitro, demonstrating that the flexible regions of D1 that protrude into the lumen can penetrate through the three side-openings of Deg1 and reach its internal proteolytic sites. This mode of action, facilitating cooperation between proteases on both sides of the thylakoid membranes, should be applicable to the degradation of other integral thylakoid membrane proteins as well.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Serina Endopeptidasas / Cloroplastos / Arabidopsis / Proteínas de Arabidopsis / Complejo de Proteína del Fotosistema II Idioma: En Revista: Sci Rep Año: 2018 Tipo del documento: Article País de afiliación: Israel

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Serina Endopeptidasas / Cloroplastos / Arabidopsis / Proteínas de Arabidopsis / Complejo de Proteína del Fotosistema II Idioma: En Revista: Sci Rep Año: 2018 Tipo del documento: Article País de afiliación: Israel