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Processing of a wheat light-harvesting chlorophyll a/b protein precursor by a soluble enzyme from higher plant chloroplasts

A processing activity has been identified in higher plant chloroplasts that cleaves the precursor of the light-harvesting chlorophyll a/b- binding protein (LHCP). A wheat LHCP gene previously characterized (Lamppa, G.K., G. Morelli, and N.-H. Chua, 1985. Mol. Cell Biol. 5:1370- 1378) was used to syn...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1987
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114706/
https://www.ncbi.nlm.nih.gov/pubmed/3320051
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collection PubMed
description A processing activity has been identified in higher plant chloroplasts that cleaves the precursor of the light-harvesting chlorophyll a/b- binding protein (LHCP). A wheat LHCP gene previously characterized (Lamppa, G.K., G. Morelli, and N.-H. Chua, 1985. Mol. Cell Biol. 5:1370- 1378) was used to synthesize RNA and subsequently the labeled precursor polypeptide in vitro. Incubation of the LHCP precursors with a soluble extract from lysed chloroplasts, after removal of the thylakoids and membrane vesicles, resulted in the release of a single 25-kD peptide. In contrast, when the LHCP precursors were used in an import reaction with intact pea or wheat chloroplasts, two forms (25 and 26 kD) of mature LHCP were found. The peptide released by the processing activity in the organelle-free assay comigrated with the lower molecular mass form of mature LHCP produced during import. Properties of the processing activity suggest that it is an endopeptidase. Chloroplasts from both pea and wheat, two divergent higher plants, contain the processing enzyme, suggesting its physiological importance in LHCP assembly into the thylakoids. We discuss the implications of LHCP precursor processing by a soluble enzyme that may be in the stromal compartment.
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spelling pubmed-21147062008-05-01 Processing of a wheat light-harvesting chlorophyll a/b protein precursor by a soluble enzyme from higher plant chloroplasts J Cell Biol Articles A processing activity has been identified in higher plant chloroplasts that cleaves the precursor of the light-harvesting chlorophyll a/b- binding protein (LHCP). A wheat LHCP gene previously characterized (Lamppa, G.K., G. Morelli, and N.-H. Chua, 1985. Mol. Cell Biol. 5:1370- 1378) was used to synthesize RNA and subsequently the labeled precursor polypeptide in vitro. Incubation of the LHCP precursors with a soluble extract from lysed chloroplasts, after removal of the thylakoids and membrane vesicles, resulted in the release of a single 25-kD peptide. In contrast, when the LHCP precursors were used in an import reaction with intact pea or wheat chloroplasts, two forms (25 and 26 kD) of mature LHCP were found. The peptide released by the processing activity in the organelle-free assay comigrated with the lower molecular mass form of mature LHCP produced during import. Properties of the processing activity suggest that it is an endopeptidase. Chloroplasts from both pea and wheat, two divergent higher plants, contain the processing enzyme, suggesting its physiological importance in LHCP assembly into the thylakoids. We discuss the implications of LHCP precursor processing by a soluble enzyme that may be in the stromal compartment. The Rockefeller University Press 1987-12-01 /pmc/articles/PMC2114706/ /pubmed/3320051 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Processing of a wheat light-harvesting chlorophyll a/b protein precursor by a soluble enzyme from higher plant chloroplasts
title Processing of a wheat light-harvesting chlorophyll a/b protein precursor by a soluble enzyme from higher plant chloroplasts
title_full Processing of a wheat light-harvesting chlorophyll a/b protein precursor by a soluble enzyme from higher plant chloroplasts
title_fullStr Processing of a wheat light-harvesting chlorophyll a/b protein precursor by a soluble enzyme from higher plant chloroplasts
title_full_unstemmed Processing of a wheat light-harvesting chlorophyll a/b protein precursor by a soluble enzyme from higher plant chloroplasts
title_short Processing of a wheat light-harvesting chlorophyll a/b protein precursor by a soluble enzyme from higher plant chloroplasts
title_sort processing of a wheat light-harvesting chlorophyll a/b protein precursor by a soluble enzyme from higher plant chloroplasts
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114706/
https://www.ncbi.nlm.nih.gov/pubmed/3320051