ATP-dependent and NAD-dependent modification of glutamine synthetase from Rhodospirillum rubrum in vitro
| Autor: | D L, Woehle, B A, Lueddecke, P W, Ludden |
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| Rok vydání: | 1990 |
| Předmět: |
Adenosine Diphosphate Ribose
Binding Sites Immune Sera Immunoblotting Molecular Sequence Data Malates Glutamic Acid NAD Rhodospirillum rubrum Peptide Fragments Kinetics Adenosine Triphosphate Glutamates Glutamate-Ammonia Ligase Electrophoresis Gel Two-Dimensional Electrophoresis Polyacrylamide Gel Amino Acid Sequence Phosphorus Radioisotopes |
| Zdroj: | The Journal of biological chemistry. 265(23) |
| ISSN: | 0021-9258 |
| Popis: | 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-32P]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-32P]ATP- and [alpha-32P] 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-32P]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 (Moss, J., Watkins, P.A., Stanley, S.J., Purnell, M.R., and Kidwell, W.R. (1984) J. Biol. Chem. 259, 5100-5104). A 32P-labeled protein spot comigrates with the NAD-treated glutamine synthetase spot when glutamine synthetase purified from H3 32PO4-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. |
| Databáze: | OpenAIRE |
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