ATP-dependent protein kinase activities in the oral pathogen Streptococcus mutans.
ATP-dependent protein kinase activities in the oral pathogen Streptococcus mutans.
复制标题
口腔病原体变形链球菌中 ATP 依赖性蛋白激酶活性。
DOI：
10.1002/jcb.240330303
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发表时间：
1987
影响因子：
4
通讯作者：
Jacobson,GR
中科院分区：
文献类型：
--
作者：
Mimura,CS;Poy,F;Jacobson,GR
在口腔致病菌变形链球菌的细胞膜和细胞质中检测到ATP依赖性蛋白激酶的活性。不同多肽被内源性激酶(s)磷酸化。在膜中检测到5种磷酸化蛋白，表观质量分别为82、37、22、12和10千道尔顿（KD）。在细胞质中发现了两种主要的酸稳定磷酸化蛋白。其中一个被鉴定为磷酸烯醇丙酮酸（PEP）依赖性磷酸转移酶系统（PTS）的HPr，而另一个的表观质量为61 KD。这两种蛋白都在一个丝氨酸残基上被磷酸化。果糖1,6‐二磷酸刺激HPr激酶的磷酸化，抑制61‐KD蛋白的磷酸化。相反，果糖1 -磷酸、2 -磷酸甘油酸、3 -磷酸甘油酸和磷酸二羟丙酮抑制了HPr的磷酸化，并刺激了61 - KD蛋白的磷酸化。其他几种糖酵解中间体以及无机磷酸盐抑制其中一种或两种蛋白质的磷酸化。在与ATP孵育之前，用PEP对细胞质进行预孵育可减少磷酸（丝氨酸）- HPr的形成，但不会减少61 - KD磷酸化蛋白的形成。后一种蛋白质尚未被鉴定，但其特性表明它可能是蛋白激酶本身。这些结果为一种或多种可溶性ATP依赖性蛋白激酶inS突变提供了证据，这些蛋白激酶受到糖酵解中间体的调节，并可能在该生物体的碳水化合物摄取和代谢调节中发挥作用。一个糖转运inS突变体的反馈调节模型，由变构调节激酶介导。
ATP‐dependent protein kinase activities were detected in both membrane and cytoplasmic fractions from the oral pathogenStreptococcus mutans. Different polypeptides were phosphorylated by endogenous kinase(s) in the two fractions. In membranes, five phosphoproteins were detected with apparent masses of 82, 37, 22, 12, and 10 kilodaltons (KD). In cytoplasm, two major acid‐stable phosphoproteins were found. One was identified as HPr of the, phosphoenolpyruvate (PEP)‐dependent phosphotransferase system (PTS), while the other had an apparent mass of 61 KD. Both of these proteins were phosphorylated on a seryl residue. Fructose 1,6‐bisphosphate stimulated phosphorylation of HPr by the kinase and inhibited phosphorylation of the 61‐KD protein. In contrast, fructose 1‐phosphate, 2‐phosphoglycerate, 3‐phosphoglycerate, and dihydroxyacetone phosphate inhibited phosphorylation of HPr and stimulated phosphorylation of the 61‐KD protein. Several other glycolytic intermediates as well as inorganic phosphate inhibited phosphorylation of either or both proteins. Preincubation of cytoplasm with PEP prior to incubation with ATP reduced the amount of phospho‐(seryl)‐HPr formed, but not that of the 61‐KD phosphoprotein. The latter protein has not yet been identified but has properties that suggest that it may be the protein kinase itself. These results provide evidence for one or more soluble ATP‐dependent protein kinases inS mutansthat are regulated by glycolytic intermediates and that may play a role in the modulation of carbohydrate uptake and metabolism in this organism. A model for feedback regulation of sugar transport inS mutans, mediated by an allosterically regulated kinase is presented.