title: Genetic incorporation of Nε-acetyllysine reveals a novel acetylation-sumoylation switch in yeast.
abstract: 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 Nε-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.
authors.affiliation: Department of Chemistry, Korea Advanced Institute of Science and Technology, 291 Daehak-ro, Yuseong-gu, Daejeon 34141, Republic of Korea.
authors.forename: Sang-Woo
authors.initials: SW
authors.lastname: Kim
authors.affiliation: Department of Chemistry, Korea Advanced Institute of Science and Technology, 291 Daehak-ro, Yuseong-gu, Daejeon 34141, Republic of Korea.
authors.forename: Kyung Jin
authors.initials: KJ
authors.lastname: Lee
authors.affiliation: Division of Applied Life Science and Research Institute for Life Science, Gyeongsang National University, Jinju 660-701, Republic of Korea.
authors.forename: Sinil
authors.initials: S
authors.lastname: Kim
authors.affiliation: Department of Chemistry, Korea Advanced Institute of Science and Technology, 291 Daehak-ro, Yuseong-gu, Daejeon 34141, Republic of Korea.
authors.forename: Jihyo
authors.initials: J
authors.lastname: Kim
authors.affiliation: Department of Chemistry, Korea Advanced Institute of Science and Technology, 291 Daehak-ro, Yuseong-gu, Daejeon 34141, Republic of Korea.
authors.forename: Kyukwang
authors.initials: K
authors.lastname: Cho
authors.affiliation: Division of Applied Life Science and Research Institute for Life Science, Gyeongsang National University, Jinju 660-701, Republic of Korea. Electronic address: rohyeon@gnu.ac.kr.
authors.forename: Hyeon-Su
authors.initials: HS
authors.lastname: Ro
authors.affiliation: Department of Chemistry, Korea Advanced Institute of Science and Technology, 291 Daehak-ro, Yuseong-gu, Daejeon 34141, Republic of Korea. Electronic address: hspark@kaist.ac.kr.
authors.forename: Hee-Sung
authors.initials: HS
authors.lastname: Park
mesh_terms: D000107:Acetylation; D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism; D048749:Cytokinesis / Q000235:genetics; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism; D005816:Genetic Complementation Test; D008239:Lysine / Q000235:genetics / Q000378:metabolism*; D015202:Protein Engineering / Q000379:methods*; D011499:Protein Processing, Post-Translational; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism; D058207:Sumoylation; D058615:Synthetic Biology / Q000379:methods
chemical_list: C099502:CDC11 protein, S cerevisiae; D018797:Cell Cycle Proteins; D003598:Cytoskeletal Proteins; D029701:Saccharomyces cerevisiae Proteins; D008239:Lysine