J Bacteriol Virol.  2003 Dec;33(4):293-300.

Enzymatic characterization of Mycobacterium smegmatis ADP-ribosyltransferase

• Song EK
• Lee SY
• Cho JK
• Han MK
• Lee HH

Abstract

ADP-ribosyltransferase (ADPRT) catalyzes the reaction in which the ADP-ribose moiety of beta-NAD+ is transferred to specific amino acid residues in target proteins. The ADPRT of Mycobacterium smegmatis has been known to inactivate rifampin through ADP-ribosylation. However, the enzymatic characteristics and functions of the enzyme have not been elucidated yet. In this study, the ADPRT-glutathione S-transferase (GST) fusion protein was expressed in Escherichia coli and enzymatic characteristics of the fusion protein were investigated. ADPRT-GST fusion protein was an ADPribosyltransferase that had no NAD glycohydrolase activity. ADPRT-GST fusion protein showed no self-inactivation phenomenon that is a universal nature for all NAD glycohydrolases and is important in regulating its activity. ADPRT activity of the enzyme was decreased by novobiocin and isonicotinic acid hydrazide. These results suggest that Mycobacterium smegmatis ADPRT could be regulated by a different way from other NADases and involved in bacterial physiological process through a post-translational modification of cytosolic proteins.

Keyword

Rifampin; ADP-ribosyltransferase; Mycobacterium smegmatis

MeSH Terms

Adenosine Diphosphate Ribose
ADP Ribose Transferases*
Cytosol
Escherichia coli
Isoniazid
Mycobacterium smegmatis*
Mycobacterium*
NAD+ Nucleosidase
Novobiocin
Physiological Processes
Protein Processing, Post-Translational
Rifampin
ADP Ribose Transferases
Adenosine Diphosphate Ribose
Isoniazid
NAD+ Nucleosidase
Novobiocin
Rifampin