Role of glutamine synthetase adenylylation in the self-protection of Pseudomonas syringae subsp. "tabaci" from its toxin, tabtoxinine-beta-lactam
Role of glutamine synthetase adenylylation in the self-protection of Pseudomonas syringae subsp. "tabaci" from its toxin, tabtoxinine-beta-lactam
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谷氨酰胺合成酶腺苷酸化在丁香假单胞菌亚种自我保护中的作用。
DOI:
10.1128/jb.166.1.224-229.1986
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发表时间:
1986
影响因子:
3.2
通讯作者:
P. J. Langston
中科院分区:
文献类型:
--
作者:
T. J. Knight;R. Durbin;P. J. Langston
Selected pathovars of Pseudomonas syringae produce an extracellular phytotoxin, tabtoxinine-beta-lactam, that irreversibly inhibits its known physiological target, glutamine synthetase (GS). Pseudomonas syringae subsp. "tabaci" retains significant amounts of glutamine synthetase activity during toxin production in culture. As part of our investigation of the self-protection mechanism(s) used by these pathovars, we have determined that GS becomes adenylylated after toxin production is initiated and that the serine released from the zinc-activated hydrolysis of tabtoxin is a factor in the initiation of this adenylylation. The adenylylation state of this GS was estimated to range from E5.0-7.5. The irreversible inactivation by tabtoxinine-beta-lactam of unadenylylated and adenylylated glutamine synthetase purified from P. syringae subsp. "tabaci" was investigated. Adenylylated GS was inactivated by tabtoxinine-beta-lactam at a slower rate than was unadenylylated enzyme. Adenylylated GS (E7.5-10.5) was significantly protected from this inactivation in the presence of the enzyme effectors, AMP, Ala, Gly, His, and Ser. Thus, the combination of the adenylylation of GS after toxin production is initiated and the presence of the enzyme effectors in vivo could provide part of the self-protection mechanism used by subsp. "tabaci".