Insights into the Specificity of Lysine Acetyltransferases

Tucker, Alex C.; Taylor, Keenan C.; Rank, Katherine C.; Rayment, Ivan; Escalante-Semerena, Jorge C.

doi:10.1074/jbc.M114.613901

Title: Insights into the Specificity of Lysine Acetyltransferases

Journal Article · Fri Nov 07 00:00:00 EST 2014 · Journal of Biological Chemistry

DOI:https://doi.org/10.1074/jbc.M114.613901· OSTI ID:1194221

Tucker, Alex C. ^[1]; Taylor, Keenan C. ^[2]; Rank, Katherine C. ^[2]; Rayment, Ivan ^[2]; Escalante-Semerena, Jorge C. ^[1]

Univ. of Georgia, Athens, GA (United States). Dept. of Microbiology
Univ. of Wisconsin, Madison, WI (United States). Dept. of Biochemistry

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.

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Research Organization:: Univ. of Georgia, Athens, GA (United States); Univ. of Wisconsin, Madison, WI (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER); National Inst. of Health (NIH) (United States)

Grant/Contract Number:: AC02-06CH11357; GM062203; GM083987; T32-GM07215

OSTI ID:: 1194221

Journal Information:: Journal of Biological Chemistry, Vol. 289, Issue 52; ISSN 0021-9258

Publisher:: American Society for Biochemistry and Molecular BiologyCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 13 works

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