集胞藻属聚球藻7942菌株中PII蛋白（glnB基因产物）的磷酸化作用：体外激酶活性分析
Phosphorylation of the PII protein (glnB gene product) in the cyanobacterium Synechococcus sp. strain PCC 7942: analysis of in vitro kinase activity.
作者信息
Forchhammer K, Tandeau de Marsac N
机构信息
Lehrstuhl für Mikrobiologie, Universität München, Germany.
出版信息
J Bacteriol. 1995 Oct;177(20):5812-7. doi: 10.1128/jb.177.20.5812-5817.1995.
Abstract
The PII protein in the cyanobacterium Synechococcus sp. strain PCC 7942 signals the cellular state of nitrogen assimilation relative to CO2 fixation by being phosphorylated at a seryl residue. In this study, we first determined the location of the phosphorylated seryl residue within the PII amino acid sequence. The phosphorylation site exhibits an RXS motif, a recognition sequence characteristic for cyclic AMP-dependent protein serine kinases from eukaryotes. We established an in vitro PII phosphorylation assay to further analyze the PII kinase activity in Synechococcus sp. strain PCC 7942. ATP was used specifically as a phosphoryl donor, and the PII kinase activity was shown to be stimulated by alpha-ketoglutarate. Unlike the PII-modifying uridylyltransferase- and uridylyl-removing enzyme characterized in proteobacteria, the activity of the PII kinase from the cyanobacterium did not respond to glutamine.
摘要
蓝藻聚球藻属菌株PCC 7942中的PII蛋白通过在丝氨酸残基处被磷酸化，来表明相对于二氧化碳固定的氮同化细胞状态。在本研究中，我们首先确定了磷酸化丝氨酸残基在PII氨基酸序列中的位置。磷酸化位点呈现RXS基序，这是真核生物中依赖环磷酸腺苷的蛋白丝氨酸激酶的特征性识别序列。我们建立了体外PII磷酸化测定法，以进一步分析聚球藻属菌株PCC 7942中的PII激酶活性。ATP被专门用作磷酰基供体，并且PII激酶活性显示受α-酮戊二酸刺激。与在变形菌中表征的PII修饰尿苷酰转移酶和尿苷酰去除酶不同，蓝藻中的PII激酶活性对谷氨酰胺没有反应。
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