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Journal of Biochemistry Advance Access published online on September 30, 2008
Journal of Biochemistry, doi:10.1093/jb/mvn124
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© 2008 The Japanese Biochemical Society

Establishment of glutamine synthetase of Mycobacterium smegmatis as a protein acetyltransferase utilizing polyphenolic acetates as the acetyl group donors

Garima Gupta1, Anil Singh Baghel1, Seema Bansal1, Tapesh Kumar Tyagi1, Ranju Kumari1, Neeraj Kumar Saini1, Prija Ponnan1,3, Ajit Kumar1, Mridula Bose1, Daman Saluja2, Shamkant Anant Patkar4, Virinder Singh Parmar3 and Hanumantharao Guru Raj1,*

1Department of Biochemistry and Microbiology, V.P. Chest Institute, 2Dr. B. R. Ambedkar Centre for Biomedical Research, 3Department of Chemistry, University of Delhi, Delhi-1100 07, India, 4Department of Protein Biochemistry and Enzyme Design, Novozymes A/S, Smormosvej 25, DK 2880, Bagsvaerd, Denmark

*Corresponding Author: Prof. Hanumantharao Guru Raj, PhD, Professor & Head, Department of Biochemistry, V.P. Chest Institute, University of Delhi, Delhi-1100 07,India Telephone No. 91-11-27667497 Fax No. 91-11-27667420 Email: rajhg{at}yahoo.com

Received August 20, 2008; Accepted September 11, 2008


  Abstract

Acetoxy Drug: Protein Transacetylase (TAase) mediating the transfer of acetyl group(s) from polyphenolic acetates (PA) to certain functional proteins in mammalian cells was identified by our earlier investigations. TAase activity was characterized in the cell lysates of Mycobacterium smegmatis and the purified protein was found to have Mr 58,000. TAase catalyzed protein acetylation by a model acetoxy drug 7, 8-Diacetoxy-4-methylcoumarin (DAMC) was established by the demonstration of immunoreactivity of the acetylated target protein with an anti-acetyllysine antibody. The specificity of the TAase of M. smegmatis (MTAase) to various acetoxycoumarins was found to be in the order DAMC >7-AMC >6-AMC >4-AC >3-AC >ABP. Also, the N-terminal sequence of purified MTAase was found to perfectly match with glutamine synthetase (GS) of M. smegmatis. The identity of MTAase with GS was confirmed by the observation that the purified MTAase as well as the purified recombinant GS exhibited all the properties of GS. The finding that purified E. coli GS was found to have substantial TAase activity highlighted the TAase function of GS in other bacteria. These results conclusively established for the first time the protein acetyltransferase function of GS of M. smegmatis.

Key Words: protein acetylation, glutamine synthetase, polyphenolic acetate, transacetylase, Mycobacterium smegmatis


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