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This content will become publicly available on November 7, 2015

Title: Insights into the Specificity of Lysine Acetyltransferases

Reversible lysine acetylation by protein acetyltransferases is a conserved regulatory mechanism that controls diverse cellular pathways. Gcn5-related N-acetyltransferases (GNATs), named after their founding member, are found in all domains of life. GNATs are known for their role as histone acetyltransferases, but non-histone bacterial protein acetytransferases have been identified. Only structures of GNAT complexes with short histone peptide substrates are available in databases. Given the biological importance of this modification and the abundance of lysine in polypeptides, how specificity is attained for larger protein substrates is central to understanding acetyl-lysine-regulated networks. In this paper, we report the structure of a GNAT in complex with a globular protein substrate solved to 1.9 Å. GNAT binds the protein substrate with extensive surface interactions distinct from those reported for GNAT-peptide complexes. Finally, our data reveal determinants needed for the recognition of a protein substrate and provide insight into the specificity of GNATs.
 [1] ;  [2] ;  [2] ;  [2] ;  [1]
  1. Univ. of Georgia, Athens, GA (United States). Dept. of Microbiology
  2. Univ. of Wisconsin, Madison, WI (United States). Dept. of Biochemistry
Publication Date:
OSTI Identifier:
Grant/Contract Number:
AC02-06CH11357; GM062203; GM083987; T32-GM07215
Accepted Manuscript
Journal Name:
Journal of Biological Chemistry
Additional Journal Information:
Journal Volume: 289; Journal Issue: 52; Journal ID: ISSN 0021-9258
American Society for Biochemistry and Molecular Biology
Research Org:
Univ. of Georgia, Athens, GA (United States); Univ. of Wisconsin, Madison, WI (United States)
Sponsoring Org:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23); National Inst. of Health (NIH) (United States)
Country of Publication:
United States
59 BASIC BIOLOGICAL SCIENCES; 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; Acetyl Coenzyme A (Acetyl-CoA); Bacterial Metabolism; Enzyme Inactivation; Histone Acetylase; Post-translational Modification (PTM); Substrate Specificity