Modification of glutamine synthetase in Streptomyces griseus by ADP-ribosylation and adenylylation.

Abstract:

:Addition of NH4+ to STreptomyces griseus 2682 cells grown in NO3- containing medium resulted in a rapid decline in glutamine synthetase activity due to covalent modification of the enzyme. The NH4+ promoted inactivation of the enzyme was inhibited by the ADP-ribosyltransferase inhibitor 3-methoxybenzamide. In the presence of ADP-ribosyltransferase activity the purified glutamine synthetase was also inhibited by NAD+ in a concentration-dependent manner. ADP-ribosylation of glutamine synthetase was demonstrated in vitro by showing the incorporation of labeled ADP-ribose from [alpha-32P]NAD+ into glutamine synthetase subunits. Beside ADP-ribosylation, adenylylation of glutamine synthetase was also shown in S. griseus since phosphodiesterase I treatment reactivated the enzyme in crude extracts of NH(4+)-shocked cells. Glutamine synthetase was also inhibited and modified by ATP in crude cellular extracts. These results suggest that in S. griseus 2682 ADP-ribosylation of glutamine synthetase could be an alternative modification to adenylylation to regulate glutamine synthetase activity.

authors

Penyige A,Kálmánczhelyi A,Sipos A,Ensign JC,Barabás G

doi

10.1006/bbrc.1994.2501

subject

Has Abstract

pub_date

1994-10-28 00:00:00

pages

598-605

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(84)72501-0

journal_volume

204

pub_type

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