Genetic incorporation of N-epsilon-acetyllysine reveals a novel acetylation-sumoylation switch in yeast

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The lysine acetylation of proteins plays a key role in regulating protein functions, thereby controlling a wide range of cellular processes. Despite the prevalence and significance of lysine acetylation in eukaryotes, however, its systematic study has been challenged by the technical limitations of conventional approaches for selective lysine acetylation in vivo. Here, we report the in vivo study of lysine acetylation via the genetic incorporation of N-epsilon-acetyllysine in yeast. We demonstrate that a newly discovered acetylation-sumoylation switch precisely controls the localization and cellular function of the yeast septin protein, Cdc11, during the cell cycle. This approach should facilitate the comprehensive in vivo study of lysine acetylation across a wide range of proteins in eukaryotic organisms. This article is part of a Special Issue entitled "Biochemistry of Synthetic Biology - Recent Developments" Guest Editor: Dr. Ilka Heinemann and Dr. Patrick O'Donoghue. (c) 2017 Elsevier B.V. All rights reserved.
Publisher
ELSEVIER SCIENCE BV
Issue Date
2017-11
Language
English
Article Type
Article
Keywords

SACCHAROMYCES-CEREVISIAE; CELL-CYCLE; IN-VITRO; PROTEIN; SEPTIN; SITE; PHOSPHOSERINE; LOCALIZATION; SELECTION; STRATEGY

Citation

BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, v.1861, no.11, pp.3030 - 3037

ISSN
0304-4165
DOI
10.1016/j.bbagen.2017.02.002
URI
http://hdl.handle.net/10203/228607
Appears in Collection
CH-Journal Papers(저널논문)
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