Journal
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
Volume 1861, Issue 11, Pages 3030-3037Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbagen.2017.02.002
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Funding
- National Research Foundation of Korea [KAIST Systems Healthcare]
- Ministry of Education of the Republic Korea [the BK21 plus program]
- National Research Foundation of Korea [2014M3A6A4075060]
- National Research Foundation of Korea [2014M3A6A4075060] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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.
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