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Identification of Pex13p a peroxisomal membrane receptor for the PTS1 recognition factor

We have identified an S. cerevisiae integral peroxisomal membrane protein of M of 42,705 (Pex13p) that is a component of the peroxisomal protein import apparatus. Pex13p's most striking feature is an src homology 3 (SH3) domain that interacts directly with yeast Pex5p (former Pas10p), the recog...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1996
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2121012/
https://www.ncbi.nlm.nih.gov/pubmed/8858167
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description We have identified an S. cerevisiae integral peroxisomal membrane protein of M of 42,705 (Pex13p) that is a component of the peroxisomal protein import apparatus. Pex13p's most striking feature is an src homology 3 (SH3) domain that interacts directly with yeast Pex5p (former Pas10p), the recognition factor for the COOH-terminal tripeptide signal sequence (PTS1), but not with Pex7p (former Pas7p), the recognition factor for the NH2-terminal nonapeptide signal (PTS2) of peroxisomal matrix proteins. Hence, Pex13p serves as peroxisomal membrane receptor for at least one of the two peroxisomal signal recognition factors. Cells deficient in Pex13p are unable to import peroxisomal matrix proteins containing PTS1 and, surprisingly, also those containing PTS2. Pex13p deficient cells retain membranes containing the peroxisomal membrane protein Pex11p (former Pmp27p), consistent with the existence of independent pathways for the integration of peroxisomal membrane proteins and for the translocation of peroxisomal matrix proteins.
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spelling pubmed-21210122008-05-01 Identification of Pex13p a peroxisomal membrane receptor for the PTS1 recognition factor J Cell Biol Articles We have identified an S. cerevisiae integral peroxisomal membrane protein of M of 42,705 (Pex13p) that is a component of the peroxisomal protein import apparatus. Pex13p's most striking feature is an src homology 3 (SH3) domain that interacts directly with yeast Pex5p (former Pas10p), the recognition factor for the COOH-terminal tripeptide signal sequence (PTS1), but not with Pex7p (former Pas7p), the recognition factor for the NH2-terminal nonapeptide signal (PTS2) of peroxisomal matrix proteins. Hence, Pex13p serves as peroxisomal membrane receptor for at least one of the two peroxisomal signal recognition factors. Cells deficient in Pex13p are unable to import peroxisomal matrix proteins containing PTS1 and, surprisingly, also those containing PTS2. Pex13p deficient cells retain membranes containing the peroxisomal membrane protein Pex11p (former Pmp27p), consistent with the existence of independent pathways for the integration of peroxisomal membrane proteins and for the translocation of peroxisomal matrix proteins. The Rockefeller University Press 1996-10-01 /pmc/articles/PMC2121012/ /pubmed/8858167 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
Identification of Pex13p a peroxisomal membrane receptor for the PTS1 recognition factor
title Identification of Pex13p a peroxisomal membrane receptor for the PTS1 recognition factor
title_full Identification of Pex13p a peroxisomal membrane receptor for the PTS1 recognition factor
title_fullStr Identification of Pex13p a peroxisomal membrane receptor for the PTS1 recognition factor
title_full_unstemmed Identification of Pex13p a peroxisomal membrane receptor for the PTS1 recognition factor
title_short Identification of Pex13p a peroxisomal membrane receptor for the PTS1 recognition factor
title_sort identification of pex13p a peroxisomal membrane receptor for the pts1 recognition factor
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2121012/
https://www.ncbi.nlm.nih.gov/pubmed/8858167