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Disrupted yeast mitochondria can import precursor proteins directly through their inner membrane
Import of precursor proteins into the yeast mitochondrial matrix can occur directly across the inner membrane. First, disruption of the outer membrane restores protein import to mitochondria whose normal import sites have been blocked by an antibody against the outer membrane or by a chimeric, incom...
Formato: | Texto |
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Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1989
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115710/ https://www.ncbi.nlm.nih.gov/pubmed/2668297 |
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collection | PubMed |
description | Import of precursor proteins into the yeast mitochondrial matrix can occur directly across the inner membrane. First, disruption of the outer membrane restores protein import to mitochondria whose normal import sites have been blocked by an antibody against the outer membrane or by a chimeric, incompletely translocated precursor protein. Second, a potential- and ATP-dependent import of authentic or artificial precursor proteins is observed with purified inner membrane vesicles virtually free of outer membrane components. Third, import into purified inner membrane vesicles is insensitive to antibody against the outer membrane. Thus, while outer membrane components are clearly required in vivo, the inner membrane contains a complete protein translocation system that can operate by itself if the outer membrane barrier is removed. |
format | Text |
id | pubmed-2115710 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1989 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21157102008-05-01 Disrupted yeast mitochondria can import precursor proteins directly through their inner membrane J Cell Biol Articles Import of precursor proteins into the yeast mitochondrial matrix can occur directly across the inner membrane. First, disruption of the outer membrane restores protein import to mitochondria whose normal import sites have been blocked by an antibody against the outer membrane or by a chimeric, incompletely translocated precursor protein. Second, a potential- and ATP-dependent import of authentic or artificial precursor proteins is observed with purified inner membrane vesicles virtually free of outer membrane components. Third, import into purified inner membrane vesicles is insensitive to antibody against the outer membrane. Thus, while outer membrane components are clearly required in vivo, the inner membrane contains a complete protein translocation system that can operate by itself if the outer membrane barrier is removed. The Rockefeller University Press 1989-08-01 /pmc/articles/PMC2115710/ /pubmed/2668297 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 Disrupted yeast mitochondria can import precursor proteins directly through their inner membrane |
title | Disrupted yeast mitochondria can import precursor proteins directly through their inner membrane |
title_full | Disrupted yeast mitochondria can import precursor proteins directly through their inner membrane |
title_fullStr | Disrupted yeast mitochondria can import precursor proteins directly through their inner membrane |
title_full_unstemmed | Disrupted yeast mitochondria can import precursor proteins directly through their inner membrane |
title_short | Disrupted yeast mitochondria can import precursor proteins directly through their inner membrane |
title_sort | disrupted yeast mitochondria can import precursor proteins directly through their inner membrane |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115710/ https://www.ncbi.nlm.nih.gov/pubmed/2668297 |