Enzymatic characterization of Mycobacterium smegmatis ADP-ribosyltransferase
Journal of Bacteriology and Virology
;
: 293-300, 2003.
Article
Dans Coréen
| WPRIM
| ID: wpr-128194
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.
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
Sujet Principal:
Rifampicine
/
Adénosine diphosphate ribose
/
Maturation post-traductionnelle des protéines
/
Novobiocine
/
ADP ribose transferases
/
NAD nucleosidase
/
Mycobacterium smegmatis
/
Cytosol
/
Escherichia coli
/
Phénomènes physiologiques
langue:
Coréen
Texte intégral:
Journal of Bacteriology and Virology
Année:
2003
Type:
Article
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