The diversity of acetylated proteins.

Genome Biol

Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642, USA.

Published: July 2002

AI Article Synopsis

  • Acetylation of proteins is a process where acetyl groups are added to specific amino acids, facilitated by enzymes called acetyltransferases.
  • Amino-terminal acetylation is common in eukaryotic proteins and regulatory peptides, while lysine acetylation happens at various sites on numerous proteins, including histones and transcription factors.
  • This modification plays a crucial role in regulating protein function and interactions within cells.

Article Abstract

Acetylation of proteins, either on various amino-terminal residues or on the epsilon-amino group of lysine residues, is catalyzed by a wide range of acetyltransferases. Amino-terminal acetylation occurs on the bulk of eukaryotic proteins and on regulatory peptides, whereas lysine acetylation occurs at different positions on a variety of proteins, including histones, transcription factors, nuclear import factors, and alpha-tubulin.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC139359PMC
http://dx.doi.org/10.1186/gb-2002-3-5-reviews0006DOI Listing

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