Cloning and characterization of NAD-dependent protein deacetylase (Rv1151c) from Mycobacterium tuberculosis

Jing Gu; Jiao Yu Deng; Ru Li; Hongping Wei; Zhiping Zhang; Yafeng Zhou; Ying Zhang; Xian En Zhang

doi:10.1134/S0006297909070062

Cloning and characterization of NAD-dependent protein deacetylase (Rv1151c) from Mycobacterium tuberculosis

Jing Gu, Jiao Yu Deng, Ru Li, Hongping Wei, Zhiping Zhang, Yafeng Zhou, Ying Zhang, Xian En Zhang

Research output: Contribution to journal › Article › peer-review

21 Scopus citations

Abstract

Sir2 family proteins are highly conserved and catalyze a well-characterized NAD-dependent protein deacetylation reaction that regulates multiple cellular processes including aging, gene silencing, cellular differentiation, and metabolic pathways. Little is known about Sir2 family proteins in bacteria. The Sir2 homolog Rv1151c of Mycobacterium tuberculosis was cloned and over-expressed in Escherichia coli, and the protein then purified by Ni²⁺-affinity chromatography to homogeneity. The purified recombinant protein showed a typical NAD-dependent protein deacetylase activity that could be inhibited by nicotinamide and other known Sir2 inhibitors. The optimal temperature and pH for activity of Rv1151c are 25°C and pH 9 ± 1, respectively. Rv1151c is capable of deacetylating the acetyl-CoA synthetase from M. tuberculosis. However, unlike Sir2 family proteins identified from other bacteria, Rv1151c shows a substrate-independent NAD glycohydrolase activity in accordance with its auto-ADP ribosylation activity.

Original language	English (US)
Pages (from-to)	743-748
Number of pages	6
Journal	Biochemistry (Moscow)
Volume	74
Issue number	7
DOIs	https://doi.org/10.1134/S0006297909070062
State	Published - Jul 2009
Externally published	Yes

Keywords

ADP-ribosyltransferase
Deacetylase
Mycobacterium tuberculosis
NAD glycohydrolase
Sir2

ASJC Scopus subject areas

Biochemistry

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10.1134/S0006297909070062

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title = "Cloning and characterization of NAD-dependent protein deacetylase (Rv1151c) from Mycobacterium tuberculosis",

abstract = "Sir2 family proteins are highly conserved and catalyze a well-characterized NAD-dependent protein deacetylation reaction that regulates multiple cellular processes including aging, gene silencing, cellular differentiation, and metabolic pathways. Little is known about Sir2 family proteins in bacteria. The Sir2 homolog Rv1151c of Mycobacterium tuberculosis was cloned and over-expressed in Escherichia coli, and the protein then purified by Ni2+-affinity chromatography to homogeneity. The purified recombinant protein showed a typical NAD-dependent protein deacetylase activity that could be inhibited by nicotinamide and other known Sir2 inhibitors. The optimal temperature and pH for activity of Rv1151c are 25°C and pH 9 ± 1, respectively. Rv1151c is capable of deacetylating the acetyl-CoA synthetase from M. tuberculosis. However, unlike Sir2 family proteins identified from other bacteria, Rv1151c shows a substrate-independent NAD glycohydrolase activity in accordance with its auto-ADP ribosylation activity.",

keywords = "ADP-ribosyltransferase, Deacetylase, Mycobacterium tuberculosis, NAD glycohydrolase, Sir2",

author = "Jing Gu and Deng, {Jiao Yu} and Ru Li and Hongping Wei and Zhiping Zhang and Yafeng Zhou and Ying Zhang and Zhang, {Xian En}",

note = "Funding Information: Jiao Yu Deng was supported by the National 973 project (No. 030403). Ying Zhang was supported by NIH grant AI44063. The others were supported by TB Research Projects of the Chinese Academy of Sciences (No. 010405).",

year = "2009",

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doi = "10.1134/S0006297909070062",

language = "English (US)",

volume = "74",

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T1 - Cloning and characterization of NAD-dependent protein deacetylase (Rv1151c) from Mycobacterium tuberculosis

AU - Gu, Jing

AU - Deng, Jiao Yu

AU - Li, Ru

AU - Wei, Hongping

AU - Zhang, Zhiping

AU - Zhou, Yafeng

AU - Zhang, Ying

AU - Zhang, Xian En

N1 - Funding Information: Jiao Yu Deng was supported by the National 973 project (No. 030403). Ying Zhang was supported by NIH grant AI44063. The others were supported by TB Research Projects of the Chinese Academy of Sciences (No. 010405).

PY - 2009/7

Y1 - 2009/7

N2 - Sir2 family proteins are highly conserved and catalyze a well-characterized NAD-dependent protein deacetylation reaction that regulates multiple cellular processes including aging, gene silencing, cellular differentiation, and metabolic pathways. Little is known about Sir2 family proteins in bacteria. The Sir2 homolog Rv1151c of Mycobacterium tuberculosis was cloned and over-expressed in Escherichia coli, and the protein then purified by Ni2+-affinity chromatography to homogeneity. The purified recombinant protein showed a typical NAD-dependent protein deacetylase activity that could be inhibited by nicotinamide and other known Sir2 inhibitors. The optimal temperature and pH for activity of Rv1151c are 25°C and pH 9 ± 1, respectively. Rv1151c is capable of deacetylating the acetyl-CoA synthetase from M. tuberculosis. However, unlike Sir2 family proteins identified from other bacteria, Rv1151c shows a substrate-independent NAD glycohydrolase activity in accordance with its auto-ADP ribosylation activity.

AB - Sir2 family proteins are highly conserved and catalyze a well-characterized NAD-dependent protein deacetylation reaction that regulates multiple cellular processes including aging, gene silencing, cellular differentiation, and metabolic pathways. Little is known about Sir2 family proteins in bacteria. The Sir2 homolog Rv1151c of Mycobacterium tuberculosis was cloned and over-expressed in Escherichia coli, and the protein then purified by Ni2+-affinity chromatography to homogeneity. The purified recombinant protein showed a typical NAD-dependent protein deacetylase activity that could be inhibited by nicotinamide and other known Sir2 inhibitors. The optimal temperature and pH for activity of Rv1151c are 25°C and pH 9 ± 1, respectively. Rv1151c is capable of deacetylating the acetyl-CoA synthetase from M. tuberculosis. However, unlike Sir2 family proteins identified from other bacteria, Rv1151c shows a substrate-independent NAD glycohydrolase activity in accordance with its auto-ADP ribosylation activity.

KW - ADP-ribosyltransferase

KW - Deacetylase

KW - Mycobacterium tuberculosis

KW - NAD glycohydrolase

KW - Sir2

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Cloning and characterization of NAD-dependent protein deacetylase (Rv1151c) from Mycobacterium tuberculosis

Abstract

Keywords

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