Untitled

Abstract

Acetylation of proteins, either on various amino-terminal residues or on the 0-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 ,-tubulin. The electronic version of this article is the complete one and can be found online at http://genomebiology.com/2002/3/5/reviews/0006 © BioMed Central Ltd (Print ISSN 1465-6906; Online ISSN 1465-6914) Modification of proteins extends the range of possible molecular structures beyond the limits imposed by the 20 encoded amino acids and, if reversible, gives a means of control and signaling. Many proteins are acetylated, both coand post-translationally, and at least for eukaryotic proteins, acetylation is the most common covalent modification out of over 200 types that have been reported. Acetylation of proteins is catalyzed by a wide range of acetyltransferases that transfer acetyl groups from acetyl-coenzyme A to either the ,-amino group of amino-terminal residues or to the 0-amino group of lysine residues at various positions. (The ,-amino group designates the position of the central carbon atom of amino acids, whereas the 0-amino group of lysine residues designates the position of a carbon atom in the side chain.) As shown in Table 1, amino-terminal acetylation occurs cotranslationally on the bulk of acetylated eukaryotic proteins [1-3] and post-translationally on prokaryotic ribosomal proteins [4,5] and on processed eukaryotic regulatory peptides [6]. Amino-terminal acetylation is one of the most common protein modifications in eukaryotes, occurring on approximately 85% of eukaryotic proteins, but is rare for prokaryotic proteins [1][2][3]. Furthermore, 0-lysine acetylation occurs post-translationally on histones, high mobility group (HMG) proteins, transcription factors, nuclear receptors [7][8][9], and ,-tubulin [10]. Acetylation affects many protein functions, including enzymatic activity, stability, DNA binding, protein-protein interaction, and peptide-receptor recognition, and occurs on numerous and diverse proteins. Amino-terminal acetylation Cotranslational amino-terminal acetylation of eukaryotic proteinsStudies in vitro indicate that amino-terminal acetylation of eukaryotic proteins takes place when there are between 20 and 50 residues protruding from the ribosome [1,11]. Proteins susceptible to amino-terminal acetylation have a variety of different amino-terminal sequences, with no simple consensus motifs and no dependence on a single type of residue [1,3,12]. Proteins with serine and alanine termini are the most frequently acetylated, and these residues, along with methionine, glycine, and threonine, account for over 95% of the amino-terminal acetylated residues [1,2]. Only subsets of proteins with any of these amino-terminal residues are acetylated, however, and none of ...

Role of the Nuclear Receptor Coactivator AIB1-Δ4 Splice Variant in the Control of Gene Transcription

“…We also included predicted precursors that could appear as a result of cotranslational modifications such as N-terminal acetylation. In eukaryotes, 80% of all proteins have been described with an acetyl moiety added to the N terminus (24,25). Interestingly, we observed only one predicted peptide 224 MQCFALSQPR that retained an initiator methionine, which was Met 224 .…”

Trypanosoma cruzi Bromodomain Factor 3 Binds Acetylated α-Tubulin and Concentrates in the Flagellum during Metacyclogenesis

“…In 2000, Kouzarides proposed that acetylation might rival phosphorylation as a regulator of cell function and that the bromodomain may be analogous to the phosphotyrosine-recognizing SH2 domain (46). The presence of TcBDF3 outside the nucleus opens new perspectives for a possible role of lysine acetylation as a regulatory switch in complex cellular processes, as proposed by many authors (47)(48)(49)(50).…”

Functional Analysis of Early Secreted Antigenic Target-6, the Dominant T-cell Antigen of Mycobacterium tuberculosis, Reveals Key Residues Involved in Secretion, Complex Formation, Virulence, and Immunogenicity

“…Acetylation affects diverse protein functions like enzyme activity, stability, and protein-protein interactions (30) but the role of the acetylation of ESAT-6 during infection with M. tuberculosis is not known. This was one of the reasons why we constructed mutant strain H37Rv⌬RD1::2F9EsxA-T2H, which had the threonine replaced by histidine.…”