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

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 iden...

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Main Authors:	Prija Ponnan, Ajit Kumar, Prabhjot Singh, Prachi Gupta, Rini Joshi, Marco Gaspari, Luciano Saso, Ashok K. Prasad, Ramesh C. Rastogi, Virinder S. Parmar, Hanumantharao G. Raj
Format:	Article
Language:	English
Published:	Hindawi Limited 2014-01-01
Series:	The Scientific World Journal
Online Access:	http://dx.doi.org/10.1155/2014/578956

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spelling	doaj-1ef4704437cb481a8716a9cec8d7afe02020-11-25T01:40:37ZengHindawi LimitedThe Scientific World Journal2356-61401537-744X2014-01-01201410.1155/2014/578956578956Comparison of Protein Acetyltransferase Action of CRTAase with the Prototypes of HATPrija Ponnan0Ajit Kumar1Prabhjot Singh2Prachi Gupta3Rini Joshi4Marco Gaspari5Luciano Saso6Ashok K. Prasad7Ramesh C. Rastogi8Virinder S. Parmar9Hanumantharao G. Raj10Department of Biochemistry, V.P. Chest Institute, University of Delhi, Delhi 110007, IndiaDepartment of Biochemistry, V.P. Chest Institute, University of Delhi, Delhi 110007, IndiaDepartment of Biochemistry, V.P. Chest Institute, University of Delhi, Delhi 110007, IndiaDepartment of Biochemistry, V.P. Chest Institute, University of Delhi, Delhi 110007, IndiaDepartment of Biochemistry, V.P. Chest Institute, University of Delhi, Delhi 110007, IndiaDipartimento di Medicina Sperimentale e Clinica, Università di Catanzaro “Magna Graecia” Campus “S. Venuta”, Località Germaneto, 88100 Catanzaro, ItalyDepartment of Human Physiology and Pharmacology “Vittorio Erspamer”, Sapienza University of Rome, Piazzale Aldo Moro 5, 00185 Rome, ItalyDepartment of Chemistry, University of Delhi, Delhi 110007, IndiaDepartment of Chemistry, University of Delhi, Delhi 110007, IndiaDepartment of Chemistry, University of Delhi, Delhi 110007, IndiaDepartment of Biochemistry, V.P. Chest Institute, University of Delhi, Delhi 110007, IndiaOur 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.http://dx.doi.org/10.1155/2014/578956
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Prija Ponnan Ajit Kumar Prabhjot Singh Prachi Gupta Rini Joshi Marco Gaspari Luciano Saso Ashok K. Prasad Ramesh C. Rastogi Virinder S. Parmar Hanumantharao G. Raj
spellingShingle	Prija Ponnan Ajit Kumar Prabhjot Singh Prachi Gupta Rini Joshi Marco Gaspari Luciano Saso Ashok K. Prasad Ramesh C. Rastogi Virinder S. Parmar Hanumantharao G. Raj Comparison of Protein Acetyltransferase Action of CRTAase with the Prototypes of HAT The Scientific World Journal
author_facet	Prija Ponnan Ajit Kumar Prabhjot Singh Prachi Gupta Rini Joshi Marco Gaspari Luciano Saso Ashok K. Prasad Ramesh C. Rastogi Virinder S. Parmar Hanumantharao G. Raj
author_sort	Prija Ponnan
title	Comparison of Protein Acetyltransferase Action of CRTAase with the Prototypes of HAT
title_short	Comparison of Protein Acetyltransferase Action of CRTAase with the Prototypes of HAT
title_full	Comparison of Protein Acetyltransferase Action of CRTAase with the Prototypes of HAT
title_fullStr	Comparison of Protein Acetyltransferase Action of CRTAase with the Prototypes of HAT
title_full_unstemmed	Comparison of Protein Acetyltransferase Action of CRTAase with the Prototypes of HAT
title_sort	comparison of protein acetyltransferase action of crtaase with the prototypes of hat
publisher	Hindawi Limited
series	The Scientific World Journal
issn	2356-6140 1537-744X
publishDate	2014-01-01
description	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.
url	http://dx.doi.org/10.1155/2014/578956
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Comparison of Protein Acetyltransferase Action of CRTAase with the Prototypes of HAT

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