Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

ATP-dependent and NAD-dependent modification of glutamine synthetase from Rhodospirillum rubrum in vitro

Journal Article · · Journal of Biological Chemistry; (USA)
OSTI ID:6532140
Glutamine synthetase from the photosynthetic bacterium Rhodospirillum rubrum is the target of both ATP- and NAD-dependent modification. Incubation of R. rubrum cell supernatant with ({alpha}-{sup 32}P)NAD results in the labeling of glutamine synthetase and two other unidentified proteins. Dinitrogenase reductase ADP-ribosyltransferase does not appear to be responsible for the modification of glutamine synthetase or the unidentified proteins. The ({alpha}-{sup 32}P)ATP- and ({alpha}-{sup 32}P) NAD-dependent modifications of R. rubrum glutamine synthetase appear to be exclusive and the two forms of modified glutamine synthetase are separable on two-dimensional gels. Loss of enzymatic activity by glutamine synthetase did not correlate with ({alpha}-{sup 32}P)NAD labeling. This is in contrast to inactivation by nonphysiological ADP-ribosylation of other glutamine synthetases by an NAD:arginine ADP-ribosyltransferase from turkey erythrocytes. A {sup 32}P-labeled protein spot comigrates with the NAD-treated glutamine synthetase spot when glutamine synthetase purified from H{sub 3} {sup 32}PO{sub 4}-grown cells is analyzed on two-dimensional gels. The adenylylation site of R. rubrum glutamine synthetase has been determined to be Leu-(Asp)-Tyr-Leu-Pro-Pro-Glu-Glu-Leu-Met; the tyrosine residue is the site of modification.
OSTI ID:
6532140
Journal Information:
Journal of Biological Chemistry; (USA), Journal Name: Journal of Biological Chemistry; (USA) Vol. 265:23; ISSN JBCHA; ISSN 0021-9258
Country of Publication:
United States
Language:
English