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Identification and Functional Characterization of N-Terminally Acetylated Proteins in Drosophila melanogaster

S Goetze, E Qeli, C Mosimann, An Staes UGent, B Gerrits, B Roschitzki, S Mohanty, EM Niederer, E Laczko and Evy Timmerman UGent, et al. (2009) PLOS BIOLOGY. 7(11). p.e1000236/1-e1000236/16
abstract
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.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
SACCHAROMYCES-CEREVISIAE, ARF-LIKE GTPASE, SEQUENCE REQUIREMENTS, EUKARYOTIC PROTEINS, ESCHERICHIA-COLI, PROTEOMICS, PLASMA-PROTEINS, YEAST, METHIONINE, ACETYLTRANSFERASES
journal title
PLOS BIOLOGY
PLoS. Biol.
volume
7
issue
11
pages
16 pages
publisher
PUBLIC LIBRARY SCIENCE
place of publication
SAN FRANCISCO
Web of Science type
Article
Web of Science id
000272032000002
JCR category
BIOLOGY
JCR impact factor
12.916 (2009)
JCR rank
1/73 (2009)
JCR quartile
1 (2009)
ISSN
1544-9173
DOI
10.1371/journal.pbio.1000236
language
English
UGent publication?
yes
classification
A1
id
828195
handle
http://hdl.handle.net/1854/LU-828195
date created
2010-01-14 11:50:26
date last changed
2013-01-30 09:41:44
@article{828195,
  abstract     = {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.},
  author       = {Goetze, S and Qeli, E and Mosimann, C and Staes, An and Gerrits, B and Roschitzki, B and Mohanty, S and Niederer, EM and Laczko, E and Timmerman, Evy and Lange, V and Hafen, E and Aebersold, R and Vandekerckhove, Jo{\"e}l and Basler, K and Ahrens, CH and Gevaert, Kris and Brunner, E},
  issn         = {1544-9173},
  journal      = {PLOS BIOLOGY},
  keyword      = {SACCHAROMYCES-CEREVISIAE,ARF-LIKE GTPASE,SEQUENCE REQUIREMENTS,EUKARYOTIC PROTEINS,ESCHERICHIA-COLI,PROTEOMICS,PLASMA-PROTEINS,YEAST,METHIONINE,ACETYLTRANSFERASES},
  language     = {eng},
  number       = {11},
  pages        = {e1000236/1--e1000236/16},
  publisher    = {PUBLIC LIBRARY SCIENCE},
  title        = {Identification and Functional Characterization of N-Terminally Acetylated Proteins in Drosophila melanogaster},
  url          = {http://dx.doi.org/10.1371/journal.pbio.1000236},
  volume       = {7},
  year         = {2009},
}

Chicago
Goetze, S, E Qeli, C Mosimann, An Staes, B Gerrits, B Roschitzki, S Mohanty, et al. 2009. “Identification and Functional Characterization of N-Terminally Acetylated Proteins in Drosophila Melanogaster.” Plos Biology 7 (11): e1000236/1–e1000236/16.
APA
Goetze, S., Qeli, E., Mosimann, C., Staes, A., Gerrits, B., Roschitzki, B., Mohanty, S., et al. (2009). Identification and Functional Characterization of N-Terminally Acetylated Proteins in Drosophila melanogaster. PLOS BIOLOGY, 7(11), e1000236/1–e1000236/16.
Vancouver
1.
Goetze S, Qeli E, Mosimann C, Staes A, Gerrits B, Roschitzki B, et al. Identification and Functional Characterization of N-Terminally Acetylated Proteins in Drosophila melanogaster. PLOS BIOLOGY. SAN FRANCISCO: PUBLIC LIBRARY SCIENCE; 2009;7(11):e1000236/1–e1000236/16.
MLA
Goetze, S, E Qeli, C Mosimann, et al. “Identification and Functional Characterization of N-Terminally Acetylated Proteins in Drosophila Melanogaster.” PLOS BIOLOGY 7.11 (2009): e1000236/1–e1000236/16. Print.