title: Comparison of protein acetyltransferase action of CRTAase with the prototypes of HAT.
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.
authors.affiliation: Department of Biochemistry, V.P. Chest Institute, University of Delhi, Delhi 110007, India ; Department of Chemistry, University of Delhi, Delhi 110007, India.
authors.forename: Prija
authors.initials: P
authors.lastname: Ponnan
authors.affiliation: Department of Biochemistry, V.P. Chest Institute, University of Delhi, Delhi 110007, India ; Department of Chemistry, SRM University Haryana, Plot No. 39, RGEC, Sonepat 131029, India.
authors.forename: Ajit
authors.initials: A
authors.lastname: Kumar
authors.affiliation: Department of Biochemistry, V.P. Chest Institute, University of Delhi, Delhi 110007, India.
authors.forename: Prabhjot
authors.initials: P
authors.lastname: Singh
authors.affiliation: Department of Biochemistry, V.P. Chest Institute, University of Delhi, Delhi 110007, India.
authors.forename: Prachi
authors.initials: P
authors.lastname: Gupta
authors.affiliation: Department of Biochemistry, V.P. Chest Institute, University of Delhi, Delhi 110007, India.
authors.forename: Rini
authors.initials: R
authors.lastname: Joshi
authors.affiliation: Dipartimento di Medicina Sperimentale e Clinica, Università di Catanzaro "Magna Graecia" Campus "S. Venuta", Località Germaneto, 88100 Catanzaro, Italy.
authors.forename: Marco
authors.identifier: 0000-0002-5411-8800
authors.initials: M
authors.lastname: Gaspari
authors.affiliation: Department of Human Physiology and Pharmacology "Vittorio Erspamer", Sapienza University of Rome, Piazzale Aldo Moro 5, 00185 Rome, Italy.
authors.forename: Luciano
authors.initials: L
authors.lastname: Saso
authors.affiliation: Department of Chemistry, University of Delhi, Delhi 110007, India.
authors.forename: Ashok K
authors.initials: AK
authors.lastname: Prasad
authors.affiliation: Department of Chemistry, University of Delhi, Delhi 110007, India.
authors.forename: Ramesh C
authors.initials: RC
authors.lastname: Rastogi
authors.affiliation: Department of Chemistry, University of Delhi, Delhi 110007, India.
authors.forename: Virinder S
authors.initials: VS
authors.lastname: Parmar
authors.affiliation: Department of Biochemistry, V.P. Chest Institute, University of Delhi, Delhi 110007, India.
authors.forename: Hanumantharao G
authors.initials: HG
authors.lastname: Raj
mesh_terms: D000123:Acetyltransferases / Q000378:metabolism*; D000818:Animals; D037282:Calreticulin / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000201:enzymology; D051548:Histone Acetyltransferases / Q000378:metabolism*; D006801:Humans
chemical_list: D037282:Calreticulin; D000123:Acetyltransferases; D051548:Histone Acetyltransferases