Identification and functional characterization of N-terminally acetylated proteins in Drosophila melanogaster.

Protein modifications play a major role for most biological processes in living organisms. Amino-terminal acetylation of proteins is a common modification found throughout the tree of life: the N-terminus of a nascent polypeptide chain becomes co-translationally acetylated, often after the removal o...

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Autores principales:	Sandra Goetze, Ermir Qeli, Christian Mosimann, An Staes, Bertran Gerrits, Bernd Roschitzki, Sonali Mohanty, Eva M Niederer, Endre Laczko, Evy Timmerman, Vinzenz Lange, Ernst Hafen, Ruedi Aebersold, Joël Vandekerckhove, Konrad Basler, Christian H Ahrens, Kris Gevaert, Erich Brunner
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2009
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/175db257c04e4d4988c704d7722b31b6
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spelling	oai:doaj.org-article:175db257c04e4d4988c704d7722b31b62021-11-25T05:34:30ZIdentification and functional characterization of N-terminally acetylated proteins in Drosophila melanogaster.1544-91731545-788510.1371/journal.pbio.1000236https://doaj.org/article/175db257c04e4d4988c704d7722b31b62009-11-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19885390/pdf/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885Protein modifications play a major role for most biological processes in living organisms. Amino-terminal acetylation of proteins is a common modification found throughout the tree of life: the N-terminus of a nascent polypeptide chain becomes co-translationally acetylated, often after the removal of the initiating methionine residue. While the enzymes and protein complexes involved in these processes have been extensively studied, only little is known about the biological function of such N-terminal modification events. To identify common principles of N-terminal acetylation, we analyzed the amino-terminal peptides from proteins extracted from Drosophila Kc167 cells. We detected more than 1,200 mature protein N-termini and could show that N-terminal acetylation occurs in insects with a similar frequency as in humans. As the sole true determinant for N-terminal acetylation we could extract the (X)PX rule that indicates the prevention of acetylation under all circumstances. We could show that this rule can be used to genetically engineer a protein to study the biological relevance of the presence or absence of an acetyl group, thereby generating a generic assay to probe the functional importance of N-terminal acetylation. We applied the assay by expressing mutated proteins as transgenes in cell lines and in flies. Here, we present a straightforward strategy to systematically study the functional relevance of N-terminal acetylations in cells and whole organisms. Since the (X)PX rule seems to be of general validity in lower as well as higher eukaryotes, we propose that it can be used to study the function of N-terminal acetylation in all species.Sandra GoetzeErmir QeliChristian MosimannAn StaesBertran GerritsBernd RoschitzkiSonali MohantyEva M NiedererEndre LaczkoEvy TimmermanVinzenz LangeErnst HafenRuedi AebersoldJoël VandekerckhoveKonrad BaslerChristian H AhrensKris GevaertErich BrunnerPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 7, Iss 11, p e1000236 (2009)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Sandra Goetze Ermir Qeli Christian Mosimann An Staes Bertran Gerrits Bernd Roschitzki Sonali Mohanty Eva M Niederer Endre Laczko Evy Timmerman Vinzenz Lange Ernst Hafen Ruedi Aebersold Joël Vandekerckhove Konrad Basler Christian H Ahrens Kris Gevaert Erich Brunner Identification and functional characterization of N-terminally acetylated proteins in Drosophila melanogaster.
description	Protein modifications play a major role for most biological processes in living organisms. Amino-terminal acetylation of proteins is a common modification found throughout the tree of life: the N-terminus of a nascent polypeptide chain becomes co-translationally acetylated, often after the removal of the initiating methionine residue. While the enzymes and protein complexes involved in these processes have been extensively studied, only little is known about the biological function of such N-terminal modification events. To identify common principles of N-terminal acetylation, we analyzed the amino-terminal peptides from proteins extracted from Drosophila Kc167 cells. We detected more than 1,200 mature protein N-termini and could show that N-terminal acetylation occurs in insects with a similar frequency as in humans. As the sole true determinant for N-terminal acetylation we could extract the (X)PX rule that indicates the prevention of acetylation under all circumstances. We could show that this rule can be used to genetically engineer a protein to study the biological relevance of the presence or absence of an acetyl group, thereby generating a generic assay to probe the functional importance of N-terminal acetylation. We applied the assay by expressing mutated proteins as transgenes in cell lines and in flies. Here, we present a straightforward strategy to systematically study the functional relevance of N-terminal acetylations in cells and whole organisms. Since the (X)PX rule seems to be of general validity in lower as well as higher eukaryotes, we propose that it can be used to study the function of N-terminal acetylation in all species.
format	article
author	Sandra Goetze Ermir Qeli Christian Mosimann An Staes Bertran Gerrits Bernd Roschitzki Sonali Mohanty Eva M Niederer Endre Laczko Evy Timmerman Vinzenz Lange Ernst Hafen Ruedi Aebersold Joël Vandekerckhove Konrad Basler Christian H Ahrens Kris Gevaert Erich Brunner
author_facet	Sandra Goetze Ermir Qeli Christian Mosimann An Staes Bertran Gerrits Bernd Roschitzki Sonali Mohanty Eva M Niederer Endre Laczko Evy Timmerman Vinzenz Lange Ernst Hafen Ruedi Aebersold Joël Vandekerckhove Konrad Basler Christian H Ahrens Kris Gevaert Erich Brunner
author_sort	Sandra Goetze
title	Identification and functional characterization of N-terminally acetylated proteins in Drosophila melanogaster.
title_short	Identification and functional characterization of N-terminally acetylated proteins in Drosophila melanogaster.
title_full	Identification and functional characterization of N-terminally acetylated proteins in Drosophila melanogaster.
title_fullStr	Identification and functional characterization of N-terminally acetylated proteins in Drosophila melanogaster.
title_full_unstemmed	Identification and functional characterization of N-terminally acetylated proteins in Drosophila melanogaster.
title_sort	identification and functional characterization of n-terminally acetylated proteins in drosophila melanogaster.
publisher	Public Library of Science (PLoS)
publishDate	2009
url	https://doaj.org/article/175db257c04e4d4988c704d7722b31b6
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Identification and functional characterization of N-terminally acetylated proteins in Drosophila melanogaster.

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