固氮细菌巴西固氮螺菌中的（甲基）铵转运
(Methyl)ammonium transport in the nitrogen-fixing bacterium Azospirillum brasilense.
作者信息
Van Dommelen A, Keijers V, Vanderleyden J, de Zamaroczy M
机构信息
F. A. Janssens Laboratory of Genetics, 3001 Heverlee, Belgium.
出版信息
J Bacteriol. 1998 May;180(10):2652-9. doi: 10.1128/JB.180.10.2652-2659.1998.
Abstract
An ammonium transporter of Azospirillum brasilense was characterized. In contrast to most previously reported putative prokaryotic NH4+ transporter genes, A. brasilense amtB is not part of an operon with glnB or glnZ which, in A. brasilense, encode nitrogen regulatory proteins PII and PZ, respectively. Sequence analysis predicts the presence of 12 transmembrane domains in the deduced AmtB protein and classifies AmtB as an integral membrane protein. Nitrogen regulates the transcription of the amtB gene in A. brasilense by the Ntr system. amtB is the first gene identified in A. brasilense whose expression is regulated by NtrC. The observation that ammonium uptake is still possible in mutants lacking the AmtB protein suggests the presence of a second NH4+ transport mechanism. Growth of amtB mutants at low ammonium concentrations is reduced compared to that of the wild type. This suggests that AmtB has a role in scavenging ammonium at low concentrations.
摘要
对巴西固氮螺菌的一种铵转运蛋白进行了表征。与大多数先前报道的假定原核生物NH4+转运蛋白基因不同，巴西固氮螺菌amtB不是与glnB或glnZ组成操纵子的一部分，在巴西固氮螺菌中，glnB和glnZ分别编码氮调节蛋白PII和PZ。序列分析预测推导的AmtB蛋白中存在12个跨膜结构域，并将AmtB分类为整合膜蛋白。氮通过Ntr系统调节巴西固氮螺菌中amtB基因的转录。amtB是在巴西固氮螺菌中鉴定出的第一个其表达受NtrC调节的基因。缺乏AmtB蛋白的突变体仍能吸收铵，这一观察结果表明存在第二种NH4+转运机制。与野生型相比，amtB突变体在低铵浓度下的生长受到抑制。这表明AmtB在低浓度下清除铵方面发挥作用。
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