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The Scientific World Journal
Volume 2014 (2014), Article ID 578956, 9 pages
http://dx.doi.org/10.1155/2014/578956
Review Article

Comparison of Protein Acetyltransferase Action of CRTAase with the Prototypes of HAT

1Department of Biochemistry, V.P. Chest Institute, University of Delhi, Delhi 110007, India
2Department of Chemistry, University of Delhi, Delhi 110007, India
3Department of Chemistry, SRM University Haryana, Plot No. 39, RGEC, Sonepat 131029, India
4Dipartimento di Medicina Sperimentale e Clinica, Università di Catanzaro “Magna Graecia” Campus “S. Venuta”, Località Germaneto, 88100 Catanzaro, Italy
5Department of Human Physiology and Pharmacology “Vittorio Erspamer”, Sapienza University of Rome, Piazzale Aldo Moro 5, 00185 Rome, Italy

Received 11 August 2013; Accepted 4 December 2013; Published 4 February 2014

Academic Editors: M. Y. Arica, D. Benke, and Y. D. Jung

Copyright © 2014 Prija Ponnan et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Our laboratory is credited for the discovery of enzymatic acetylation of protein, a phenomenon unknown till we identified an enzyme termed acetoxy drug: protein transacetylase (TAase), catalyzing the transfer of acetyl group from polyphenolic acetates to receptor proteins (RP). Later, TAase was identified as calreticulin (CR), an endoplasmic reticulum luminal protein. CR was termed calreticulin transacetylase (CRTAase). Our persistent study revealed that CR like other families of histone acetyltransferases (HATs) such as p300, Rtt109, PCAF, and ESA1, undergoes autoacetylation. The autoacetylated CR was characterized as a stable intermediate in CRTAase catalyzed protein acetylation, and similar was the case with ESA1. The autoacetylation of CR like that of HATs was found to enhance protein-protein interaction. CR like HAT-1, CBP, and p300 mediated the acylation of RP utilizing acetyl CoA and propionyl CoA as the substrates. The similarities between CRTAase and HATs in mediating protein acylation are highlighted in this review.