נגישות
menu      
חיפוש מתקדם
תחביר
חפש...
הספר "אוצר וולקני"
אודות
תנאי שימוש
ניהול
קהילה:
אסיף מאגר המחקר החקלאי
פותח על ידי קלירמאש פתרונות בע"מ -
The Protein Disulfide Isomerase-like RB60 Is Partitioned between Stroma and Thylakoids in Chlamydomonas reinhardtii Chloroplasts
Year:
2001
Source of publication :
Journal of Biological Chemistry
Authors :
אוסטרזצר, אורן
;
.
מאירי, אתי
;
.
Volume :
276
Co-Authors:
Trebitsh, T., Department of Plant Sciences, Weizmann Institute of Science, Hebrew University of Jerusalem, P. O. Box 12, Rehovot 76100, Israel
Meiri, E., Department of Plant Sciences, Weizmann Institute of Science, Hebrew University of Jerusalem, P. O. Box 12, Rehovot 76100, Israel
Ostersetzer, O., Department of Agricultural Botany, Hebrew University of Jerusalem, P. O. Box 12, Rehovot 76100, Israel
Adam, Z., Department of Agricultural Botany, Hebrew University of Jerusalem, P. O. Box 12, Rehovot 76100, Israel
Danon, A., Department of Plant Sciences, Weizmann Institute of Science, Hebrew University of Jerusalem, P. O. Box 12, Rehovot 76100, Israel
Facilitators :
From page:
4564
To page:
4569
(
Total pages:
6
)
Abstract:
Translation of psbA mRNA in Chlamydomonas reinhardtii chloroplasts is regulated by a redox signal(s). RB60 is a member of a protein complex that binds with high affinity to the 5′-untranslated region of psbA mRNA. RB60 has been suggested to act as a redox-sensor subunit of the protein complex regulating translation of chloroplast psbA mRNA. Surprisingly, cloning of RB60 identified high homology to the endoplasmic reticulum-localized protein disulfide isomerase, including an endoplasmic reticulum-retention signal at its carboxyl terminus. Here we show, by in vitro import studies, that the recombinant RB60 is imported into isolated chloroplasts of C. reinhardtii and pea in a transit peptide-dependent manner. Subtractionation of C. reinhardtii chloroplasts revealed that the native RB60 is partitioned between the stroma and the thylakoids. The nature of association of native RB60, and imported recombinant RB60, with thylakoids is similar and suggests that RB60 is tightly bound to thylakoids. The targeting characteristics of RB60 and the potential implications of the association of RB60 with thylakoids are discussed.
Note:
Related Files :
Animals
Biochemistry
cloning
enzymes
Genetics
molecular genetics
Pisum sativum
RNA
עוד תגיות
תוכן קשור
More details
DOI :
10.1074/jbc.M005950200
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
18795
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:24
You may also be interested in
Scientific Publication
The Protein Disulfide Isomerase-like RB60 Is Partitioned between Stroma and Thylakoids in Chlamydomonas reinhardtii Chloroplasts
276
Trebitsh, T., Department of Plant Sciences, Weizmann Institute of Science, Hebrew University of Jerusalem, P. O. Box 12, Rehovot 76100, Israel
Meiri, E., Department of Plant Sciences, Weizmann Institute of Science, Hebrew University of Jerusalem, P. O. Box 12, Rehovot 76100, Israel
Ostersetzer, O., Department of Agricultural Botany, Hebrew University of Jerusalem, P. O. Box 12, Rehovot 76100, Israel
Adam, Z., Department of Agricultural Botany, Hebrew University of Jerusalem, P. O. Box 12, Rehovot 76100, Israel
Danon, A., Department of Plant Sciences, Weizmann Institute of Science, Hebrew University of Jerusalem, P. O. Box 12, Rehovot 76100, Israel
The Protein Disulfide Isomerase-like RB60 Is Partitioned between Stroma and Thylakoids in Chlamydomonas reinhardtii Chloroplasts
Translation of psbA mRNA in Chlamydomonas reinhardtii chloroplasts is regulated by a redox signal(s). RB60 is a member of a protein complex that binds with high affinity to the 5′-untranslated region of psbA mRNA. RB60 has been suggested to act as a redox-sensor subunit of the protein complex regulating translation of chloroplast psbA mRNA. Surprisingly, cloning of RB60 identified high homology to the endoplasmic reticulum-localized protein disulfide isomerase, including an endoplasmic reticulum-retention signal at its carboxyl terminus. Here we show, by in vitro import studies, that the recombinant RB60 is imported into isolated chloroplasts of C. reinhardtii and pea in a transit peptide-dependent manner. Subtractionation of C. reinhardtii chloroplasts revealed that the native RB60 is partitioned between the stroma and the thylakoids. The nature of association of native RB60, and imported recombinant RB60, with thylakoids is similar and suggests that RB60 is tightly bound to thylakoids. The targeting characteristics of RB60 and the potential implications of the association of RB60 with thylakoids are discussed.
Scientific Publication
You may also be interested in