N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum.

Amino-terminal acetylation is probably the most common protein modification in eukaryotes with as many as 50%-80% of proteins reportedly altered in this way. Here we report a systematic analysis of the predicted N-terminal processing of cytosolic proteins versus those destined to be sorted to the se...

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Autores principales:	Gabriella M A Forte, Martin R Pool, Colin J Stirling
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/60376e1c97c340798328344ab8afaec3
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spelling	oai:doaj.org-article:60376e1c97c340798328344ab8afaec32021-11-18T05:36:10ZN-terminal acetylation inhibits protein targeting to the endoplasmic reticulum.1544-91731545-788510.1371/journal.pbio.1001073https://doaj.org/article/60376e1c97c340798328344ab8afaec32011-05-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21655302/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885Amino-terminal acetylation is probably the most common protein modification in eukaryotes with as many as 50%-80% of proteins reportedly altered in this way. Here we report a systematic analysis of the predicted N-terminal processing of cytosolic proteins versus those destined to be sorted to the secretory pathway. While cytosolic proteins were profoundly biased in favour of processing, we found an equal and opposite bias against such modification for secretory proteins. Mutations in secretory signal sequences that led to their acetylation resulted in mis-sorting to the cytosol in a manner that was dependent upon the N-terminal processing machinery. Hence N-terminal acetylation represents an early determining step in the cellular sorting of nascent polypeptides that appears to be conserved across a wide range of species.Gabriella M A ForteMartin R PoolColin J StirlingPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 9, Iss 5, p e1001073 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Gabriella M A Forte Martin R Pool Colin J Stirling N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum.
description	Amino-terminal acetylation is probably the most common protein modification in eukaryotes with as many as 50%-80% of proteins reportedly altered in this way. Here we report a systematic analysis of the predicted N-terminal processing of cytosolic proteins versus those destined to be sorted to the secretory pathway. While cytosolic proteins were profoundly biased in favour of processing, we found an equal and opposite bias against such modification for secretory proteins. Mutations in secretory signal sequences that led to their acetylation resulted in mis-sorting to the cytosol in a manner that was dependent upon the N-terminal processing machinery. Hence N-terminal acetylation represents an early determining step in the cellular sorting of nascent polypeptides that appears to be conserved across a wide range of species.
format	article
author	Gabriella M A Forte Martin R Pool Colin J Stirling
author_facet	Gabriella M A Forte Martin R Pool Colin J Stirling
author_sort	Gabriella M A Forte
title	N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum.
title_short	N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum.
title_full	N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum.
title_fullStr	N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum.
title_full_unstemmed	N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum.
title_sort	n-terminal acetylation inhibits protein targeting to the endoplasmic reticulum.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/60376e1c97c340798328344ab8afaec3
work_keys_str_mv	AT gabriellamaforte nterminalacetylationinhibitsproteintargetingtotheendoplasmicreticulum AT martinrpool nterminalacetylationinhibitsproteintargetingtotheendoplasmicreticulum AT colinjstirling nterminalacetylationinhibitsproteintargetingtotheendoplasmicreticulum
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N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum.

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