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Protein acetylation

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Summary

The first reports of the presence of acetyl groups in proteins were concerned with N-terminal acetylation and in 1958 an acetyl peptide was found in a natural protein. The presence of acetyl groups in histories was reported in 1963. N-terminal acetylation can occur in the absence of protein biosynthesis in cell-free systems, although the N-terminus became acetylated while the chain was still on the ribosome. After in vivo administration of 3H-acetate, a displacement of the radioactivity with time towards the higher molecular weight regions is evident. The acetyl groups are bound in the peptidyl moiety of the peptidyl-tRNA. N-terminal acetylation of the H4 histories occurs on the nascent chains in the cytoplasm, whereas internal lysine residues are progressively acetylated after the histone enters the nucleus. The H1 histories containing only the amino terminal acetyl group are the most stable metabolically.

Acetylation of chromosomal proteins has been correlated with gene activation and, also, gene inactivation has been correlated with histone deacetylation. Both processes occur rapidly and twice as fast in nuclei from rat hepatoma cells as in nuclei from fetal and adult livers. The arginine-rich histone fraction appears to play a major role in the regulation of RNA synthesis and the arginine-rich histone-specific acetyl transferases may have a major function in the transcription of the genome.

Acetyl transferases have been characterized from: pigeon liver acetone fractions, cytosol of uteri from immature rats, rat liver nuclei and cytoplasm, calf liver nuclei and calf thymus cytoplasm, all with different specificities. An acetyl transferase bound to ribosomes active in the acetylation of histories can be solubilized by washing the ribosomes with 0.5 M KCI. Acetylation of ribosomal proteins occurs at a time when the initiation complex is being formed. The acetyl transferase activity of rat liver cytoplasm can be resolved into two components by gel filtration. One component appears to be responsible for acetylation of the epsilon amino group of internal lysine residues in nascent chains. The other component has been investigated to a greater extent and constitutes an RNA-containing proteolipid complex termed complex A which contains enzymes responsible for amino acid activation and the acetylation of polysomal proteins. Electron microscopic studies have revealed a duplex structure with a central hollow in the big unit. Its RNA consists largely of tRNA. The eight lipids, contained therein with the exception of two, were glycolipids. Activities for the enzymatic activation of twelve amino acids: L-Arg, L-Asp, L-Glu, L-GluNH2, Gly, L-Leu, L-Met, L-Phe, L-Pro, L-Ser, L-Thr and L-Tyr may be located on the inside of complex A, while lysine

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Author notes

  1. A. Pestana

    Present address: Facultad de Medicina de la Universidad Autonoma, Instituto de Enzymologia del C.S.I.C., 34, Madrid, Spain

Authors and Affiliations

  1. Dept. of Oncology, Medical School, University of Wisconsin, 53706, Madison, WI, USA

    H. J. K. Saxholm, A. Pestana, L. O'Connor, C. A. Sattler & H. C. Pitot

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  1. H. J. K. Saxholm
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  2. A. Pestana
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Norwegian Cancer Society Research Fellow.

International Fellow of the National Institutes of Health (TW01627).

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Saxholm, H.J.K., Pestana, A., O'Connor, L. et al. Protein acetylation. Mol Cell Biochem 46, 129–153 (1982). https://doi.org/10.1007/BF00239663

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