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פותח על ידי קלירמאש פתרונות בע"מ -
Protein modifications in the d 2 protein of photosystem ii affect properties of the QB/herbicide-binding environment
Year:
1993
Authors :
אורן-שמיר, מיכל
;
.
Volume :
48
Co-Authors:
Kless, H., Department of Botany, Center for the Study of Early Events in Photosynthesis, Arizona State University, Arizona 85287-1601, United States
Vermaas, W., Department of Botany, Center for the Study of Early Events in Photosynthesis, Arizona State University, Arizona 85287-1601, United States
Oren-Shamir, M., Department of Plant Genetics, The Weizmann Institute of Science, Rehovot 76100, Israel
Edelman, M., Department of Plant Genetics, The Weizmann Institute of Science, Rehovot 76100, Israel
Ohadc, I., Department of Biological Chemistry, The Hebrew University of Jerusalem, Jerusalem 91904, Israel
Facilitators :
From page:
185
To page:
190
(
Total pages:
6
)
Abstract:
The D2 protein contains an extended loop (the D-de loop) between helices D and de at the reducing side of photosystem II (PS II). Characterization of D2 mutants of the cyanobacterium Synechocystis sp. PCC 6803 has indicated that the length and amino acid composition of the D-de loop are not critical for basic PS II functions, although most of the residues in that region are conserved phylogenetically. Here we show using herbicide binding and electron-flow inhibition measurements that drastic modifications in the D-de loop of the D2 protein modify the interaction of some PS II-directed herbicides with their binding niche. The stability of (semi-)reduced QB in its binding pocket is altered in at least two of the mutants, as indicated by a shifted peak temperature of the thermoluminescence signal originating from charge recombination involving QB. These results suggest a close functional association between the D-de loop of the D2 protein and the QB/herbicide-binding environment, which is viewed as being coordinated mostly by residues of the D 1 protein. This represents one of the first examples of modification of the QB/herbicide-binding domain by mutations in the D2 protein. © 1993, Walter de Gruyter. All rights reserved.
Note:
Related Files :
Binding Sites
chlorophyll
drug effect
Genetics
genetic transformation
herbicides
metabolism
molecular genetics
photosynthesis
עוד תגיות
תוכן קשור
More details
DOI :
10.1515/znc-1993-3-413
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
20529
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:37
You may also be interested in
Scientific Publication
Protein modifications in the d 2 protein of photosystem ii affect properties of the QB/herbicide-binding environment
48
Kless, H., Department of Botany, Center for the Study of Early Events in Photosynthesis, Arizona State University, Arizona 85287-1601, United States
Vermaas, W., Department of Botany, Center for the Study of Early Events in Photosynthesis, Arizona State University, Arizona 85287-1601, United States
Oren-Shamir, M., Department of Plant Genetics, The Weizmann Institute of Science, Rehovot 76100, Israel
Edelman, M., Department of Plant Genetics, The Weizmann Institute of Science, Rehovot 76100, Israel
Ohadc, I., Department of Biological Chemistry, The Hebrew University of Jerusalem, Jerusalem 91904, Israel
Protein modifications in the d 2 protein of photosystem ii affect properties of the QB/herbicide-binding environment
The D2 protein contains an extended loop (the D-de loop) between helices D and de at the reducing side of photosystem II (PS II). Characterization of D2 mutants of the cyanobacterium Synechocystis sp. PCC 6803 has indicated that the length and amino acid composition of the D-de loop are not critical for basic PS II functions, although most of the residues in that region are conserved phylogenetically. Here we show using herbicide binding and electron-flow inhibition measurements that drastic modifications in the D-de loop of the D2 protein modify the interaction of some PS II-directed herbicides with their binding niche. The stability of (semi-)reduced QB in its binding pocket is altered in at least two of the mutants, as indicated by a shifted peak temperature of the thermoluminescence signal originating from charge recombination involving QB. These results suggest a close functional association between the D-de loop of the D2 protein and the QB/herbicide-binding environment, which is viewed as being coordinated mostly by residues of the D 1 protein. This represents one of the first examples of modification of the QB/herbicide-binding domain by mutations in the D2 protein. © 1993, Walter de Gruyter. All rights reserved.
Scientific Publication
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