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פותח על ידי קלירמאש פתרונות בע"מ -
Light-stimulated degradation of an unassembled Rieske FeS protein by a thylakoid-bound protease: The possible role of the FtsH protease
Year:
1997
Source of publication :
Plant Cell
Authors :
אוסטרזצר, אורן
;
.
Volume :
9
Co-Authors:
Ostersetzer, O., Department of Agricultural Botany, Hebrew University of Jerusalem, Rehovot 76100, Israel
Adam, Z., Department of Agricultural Botany, Hebrew University of Jerusalem, Rehovot 76100, Israel
Facilitators :
From page:
957
To page:
965
(
Total pages:
9
)
Abstract:
Unassembled subunits of the cytochrome b(6)f complex as well as components of other unassembled chloroplastic complexes are rapidly degraded within the organelle. However, the mechanisms involved in these proteolytic processes are obscure. When the Rieske FeS protein (RISP) is imported into isolated chloroplasts in vitro, some of the protein does not properly assemble with the cytochrome complex, as determined by its sensitivity to exogenous protease. When assayed in intact, lysed, or fractionated chloroplasts, the imported RISP was found to be sensitive to endogenous proteases as well. The activity responsible for degradation of the unassembled protein was localized to the thylakoid membrane and characterized as a metalloprotease requiring zinc ions for its activity. The degradation rate was stimulated by light, but no involvement of ATP or redox control was observed. Instead, when the RISP that was attached to thylakoid membranes was first illuminated on ice, degradation proceeded in either light or darkness at equal rates, suggesting a light-induced conformational change making the protein prone to degradation. Antibodies raised against native FtsH, a bacterial, membrane-bound, ATP-dependent, zinc-stimulated protease, effectively inhibited degradation of the unassembled RISP, suggesting a role for the chloroplastic FtsH in this process.
Note:
Related Files :
light
metabolism
Metalloendopeptidases
seeds
temperature
Zinc
עוד תגיות
תוכן קשור
More details
DOI :
10.1105/tpc.9.6.957
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
25842
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:18
Scientific Publication
Light-stimulated degradation of an unassembled Rieske FeS protein by a thylakoid-bound protease: The possible role of the FtsH protease
9
Ostersetzer, O., Department of Agricultural Botany, Hebrew University of Jerusalem, Rehovot 76100, Israel
Adam, Z., Department of Agricultural Botany, Hebrew University of Jerusalem, Rehovot 76100, Israel
Light-stimulated degradation of an unassembled Rieske FeS protein by a thylakoid-bound protease: The possible role of the FtsH protease
Unassembled subunits of the cytochrome b(6)f complex as well as components of other unassembled chloroplastic complexes are rapidly degraded within the organelle. However, the mechanisms involved in these proteolytic processes are obscure. When the Rieske FeS protein (RISP) is imported into isolated chloroplasts in vitro, some of the protein does not properly assemble with the cytochrome complex, as determined by its sensitivity to exogenous protease. When assayed in intact, lysed, or fractionated chloroplasts, the imported RISP was found to be sensitive to endogenous proteases as well. The activity responsible for degradation of the unassembled protein was localized to the thylakoid membrane and characterized as a metalloprotease requiring zinc ions for its activity. The degradation rate was stimulated by light, but no involvement of ATP or redox control was observed. Instead, when the RISP that was attached to thylakoid membranes was first illuminated on ice, degradation proceeded in either light or darkness at equal rates, suggesting a light-induced conformational change making the protein prone to degradation. Antibodies raised against native FtsH, a bacterial, membrane-bound, ATP-dependent, zinc-stimulated protease, effectively inhibited degradation of the unassembled RISP, suggesting a role for the chloroplastic FtsH in this process.
Scientific Publication
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