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Title: Intramembrane translocation and posttranslational palmitoylation of the chloroplast 32-kDa herbicide-binding protein

Abstract

The 32-kDa herbicide-binding protein, a component of photosystem II, is synthesized as a membrane-associated 33.5-kDa precursor within the chloroplast. We show that membrane attachment of the precursor and processing to the 32-kDa form occur in the unstacked stromal lamellae. Once processed, the 32-kDa protein translocates, within the thylakoids, to the topologically distinct stacked granal lamellae. Posttranslational palmitoylation of the processed 32-kDa protein is also shown to occur. This modification takes place in a membrane-protected domain and is mainly confined to the protein assembled in the granal lamellae, where functional photosystem II centers are concentrated.

Authors:
;
Publication Date:
Research Org.:
Beltsville Agricultural Research Center, MD
OSTI Identifier:
6526174
Resource Type:
Journal Article
Journal Name:
Proc. Natl. Acad. Sci. U.S.A.; (United States)
Additional Journal Information:
Journal Volume: 6
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; PHOTOSYNTHETIC REACTION CENTERS; BIOCHEMICAL REACTION KINETICS; PROTEINS; ACYLATION; MEMBRANE TRANSPORT; CHLOROPHYLL; CHLOROPLASTS; HERBICIDES; METHIONINE; PHOTOSYNTHETIC MEMBRANES; TRACER TECHNIQUES; TRITIUM COMPOUNDS; AMINO ACIDS; CARBOXYLIC ACIDS; CELL CONSTITUENTS; CHEMICAL REACTIONS; DRUGS; HETEROCYCLIC ACIDS; HETEROCYCLIC COMPOUNDS; ISOTOPE APPLICATIONS; KINETICS; LABELLED COMPOUNDS; LIPOTROPIC FACTORS; MEMBRANES; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; ORGANIC SULFUR COMPOUNDS; PESTICIDES; PHYTOCHROMES; PIGMENTS; PORPHYRINS; REACTION KINETICS; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Mattoo, A K, and Edelman, M. Intramembrane translocation and posttranslational palmitoylation of the chloroplast 32-kDa herbicide-binding protein. United States: N. p., 1987. Web. doi:10.1073/pnas.84.6.1497.
Mattoo, A K, & Edelman, M. Intramembrane translocation and posttranslational palmitoylation of the chloroplast 32-kDa herbicide-binding protein. United States. https://doi.org/10.1073/pnas.84.6.1497
Mattoo, A K, and Edelman, M. 1987. "Intramembrane translocation and posttranslational palmitoylation of the chloroplast 32-kDa herbicide-binding protein". United States. https://doi.org/10.1073/pnas.84.6.1497.
@article{osti_6526174,
title = {Intramembrane translocation and posttranslational palmitoylation of the chloroplast 32-kDa herbicide-binding protein},
author = {Mattoo, A K and Edelman, M},
abstractNote = {The 32-kDa herbicide-binding protein, a component of photosystem II, is synthesized as a membrane-associated 33.5-kDa precursor within the chloroplast. We show that membrane attachment of the precursor and processing to the 32-kDa form occur in the unstacked stromal lamellae. Once processed, the 32-kDa protein translocates, within the thylakoids, to the topologically distinct stacked granal lamellae. Posttranslational palmitoylation of the processed 32-kDa protein is also shown to occur. This modification takes place in a membrane-protected domain and is mainly confined to the protein assembled in the granal lamellae, where functional photosystem II centers are concentrated.},
doi = {10.1073/pnas.84.6.1497},
url = {https://www.osti.gov/biblio/6526174}, journal = {Proc. Natl. Acad. Sci. U.S.A.; (United States)},
number = ,
volume = 6,
place = {United States},
year = {Sun Mar 01 00:00:00 EST 1987},
month = {Sun Mar 01 00:00:00 EST 1987}
}