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PMID: 11041889 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Insertion of OEP14 into the outer envelope membrane is mediated by proteinaceous components of chloroplasts.

The Plant cell ·Vol. 12 ·No. 10 ·2000-10-00 ·Pages 1951-60

Tu SL, Li HM

Abstract

Most chloroplastic outer envelope membrane proteins are synthesized in the cytosol at their mature size without a cleavable targeting signal. Their insertion into the outer membrane is insensitive to thermolysin pretreatment of chloroplasts and does not require ATP. The insertion has been assumed to be mediated by a spontaneous mechanism or by interaction solely with the lipid components of the outer membrane. However, we show here that insertion of an outer membrane protein requires some trypsin-sensitive and some N-ethylmaleimide-sensitive components of chloroplasts. Association and insertion of the outer membrane protein are saturable and compete with the import of another outer membrane protein. These data suggest that import of chloroplastic outer membrane proteins occurs at specific proteinaceous sites on chloroplasts.

MeSH Terms
Chloroplasts/physiology Cloning, Molecular Cytosol/metabolism Escherichia coli Intracellular Membranes/physiology Kinetics Membrane Lipids/metabolism Membrane Proteins/biosynthesis,genetics,metabolism Peas/physiology Plant Proteins/biosynthesis,genetics,metabolism Recombinant Proteins/isolation & purification,metabolism Thermolysin Trypsin
Chemicals
Membrane Lipids Membrane Proteins Plant Proteins Recombinant Proteins OM14 protein, Pisum sativum Trypsin Thermolysin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Tu S L
Graduate Institute of Life Sciences, National Defense Medical Center, Taipei 112, Taiwan.
Li H M
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35 references, click to expand
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Article Info
Journal
The Plant cell
Abbr.
Plant Cell
ISSN
1040-4651
DOI
10.1105/tpc.12.10.1951
Published
2000-10-00
Pages
1951-60
Language
English
Region
England
NLM ID
9208688
PMCID
PMC149132
Subset
IM
External Links
PubMed source DOI: 10.1105/tpc.12.10.1951 PMC Full Text View journal details
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