EurekaMag.com logo
+ Site Statistics
References:
47,893,527
Abstracts:
28,296,643
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

Regulation of glutamine synthetase ec 6.3.1.2 activity by adenylylation in the gram positive bacterium streptomyces cattleya






Proceedings of the National Academy of Sciences of the United States of America 78(1): 229-233

Regulation of glutamine synthetase ec 6.3.1.2 activity by adenylylation in the gram positive bacterium streptomyces cattleya

The enzymatic activity of glutamine synthetase [GS; L-glutamate:ammonia ligase (ADP-forming), EC 6.3.1.2] from the gram-positive bacterium S. cattleya is regulated by covalent modification. In whole cells containing high levels of GS the addition of ammonium chloride leads to a rapid decline in GS activity. Crude extracts prepared from such ammonia-shocked cells had very low levels of GS activity as measured by biosynthetic and .gamma.-glutamyltransferase assays. Incubation of the crude extracts with snake venom phosphodiesterase restored GS activity. In cell extracts, GS was also inactivated by an ATP- and glutamine-dependent reaction. Radioactive labeling studies demonstrated the incorporation of an AMP moiety into GS protein upon modification. The results suggest a covalent modification of GS in a gram-positive bacterium. This modification appears to be adenylylation of the GS subunit similar to that found in the gram-negative bacteria.


Accession: 006288127



Related references

Streicher, S.L.; Tyler, B., 1981: Regulation of glutamine synthetase activity by adenylylation in the Gram-positive bacterium Streptomyces cattleya. The enzymatic activity of glutamine synthetase [GS; L-glutamate:ammonia ligase (ADP-forming), EC 6.3.1.2] from the Gram-positive bacterium Streptomyces cattleya is regulated by covalent modification. In whole cells containing high levels of GS the...

Streicher S.L.; Tyler B., 1980: Regulation of glutamine synthetase activity by covalent modification in the gram positive bacterium streptomyces cattleya. Federation Proceedings 39(6): ABSTRACT 893

Wax, R.; Synder, L.; Kaplan, L., 1982: Inactivation of Glutamine Synthetase by Ammonia Shock in the Gram-Positive Bacterium Streptomyces cattleya. In cultures of the gram-positive bacterium Streptomyces cattleya, a rapid inactivation of glutamine synthetase was seen after ammonia shock. pH activity curves for ammonia-shocked and control cultures are shown. A peak of glutamine synthetase acti...

Wax, R.; Synder, L.; Kaplan, L., 1982: Inactivation of glutamine synthetase ec 6.3.1.2 by ammonia shock in the gram positive bacterium streptomyces cattleya. In cultures of S. cattleya, a rapid inactivtion of glutamine synthetase was seen after ammonia shock. pH activity curves for ammonia-shocked and control cultures are shown. A peak of glutamine synthetase activity was seen during fermentation for p...

Paress, P.S.; Streicher, S.L., 1985: Glutamine synthetase ec 6.3.1.2 of streptomyces cattleya purification and regulation of synthesis. Glutamine synthetase (GS) from S. cattleya was purified using a single affinity-gel chromatography step, and some of its properties were determined. Levels of GS in S. cattleya cells varied by a factor of 8 depending upon the source of N. in the g...

Paress, P.S.; Streicher, S.L., 1985: Glutamine synthetase of Streptomyces cattleya: purification and regulation of synthesis. Glutamine synthetase (GS; EC 6.3.1.2) from Streptomyces cattleya was purified using a single affinity-gel chromatography step, and some of its properties were determined. Levels of GS in S. cattleya cells varied by a factor of 8 depending upon the...

Jiang, P.; Peliska, J.A.; Ninfa, A.J., 1998: The regulation of Escherichia coli glutamine synthetase revisited: role of 2-ketoglutarate in the regulation of glutamine synthetase adenylylation state. The regulation of Escherichia coli glutamine synthetase (GS) by reversible adenylylation has provided one of the classical paradigms for signal transduction by cyclic cascades. Yet, many mechanistic features of this regulation remain to be elucida...

Kimura K.; Suzuki H.; Nakano Y., 1988: Regulation of glutamine synthetase activity by phosphorylation instead of by adenylylation. o-Phosphotyrosyl glutamine synthetase (P-GS) was isolated from highly adenylylated glutamine synthetase (AMP-GS) purified from Mycobacterium phlei, by treatment with micrococcal nuclease. The physical characteristics of P-GS were quite similar to...

Anderson, W.B.; Hennig, S.B.; Ginsburg, A.; Stadtman, E.R., 1970: Association of atp glutamine synthetase adenyly transferrase activity with the p 1 component of the glutamine synthetase ec 6.3.1.2 de adenylylation system. Proceedings of the National Academy of Sciences of the United States of America 67(3): 1417-1424

Penyige, A.; Kálmánczhelyi, A.; Sipos, A.; Ensign, J.C.; Barabás, G., 1994: Modification of glutamine synthetase in Streptomyces griseus by ADP-ribosylation and adenylylation. Addition of NH-4+ to Streptomyces griseus 2682 cells grown in NO-3-containing medium resulted in a rapid decline in glutamine synthetase activity due to covalent modification of the enzyme. The NH-4+ promoted inactivation of the enzyme was inhibit...