磷酸化
激酶
结核分枝杆菌
蛋白质组
蛋白质磷酸化
生物
基因
膨胀的
丝氨酸苏氨酸激酶
双组分调节系统
支原体
细胞生物学
细菌
计算生物学
遗传学
蛋白激酶A
肺结核
突变体
医学
抗压强度
材料科学
病理
复合材料
作者
Andrew Frando,Vishant Mahendra Boradia,Marina A. Gritsenko,Michael-Claude Beltejar,Le Zhang Day,David H. Sherman,Shuyi Ma,Jon M. Jacobs,Christoph Grundner
标识
DOI:10.1101/2022.02.17.480717
摘要
Bacterial phosphosignaling has long been synonymous with the histidine kinases of the two component systems, but many bacteria, including Mycobacterium tuberculosis (Mtb), also code for Ser/Thr protein kinases (STPKs). STPKs are the main phosphosignaling enzymes in eukaryotes, but the full extent of phosphorylation on protein Ser/Thr and Tyr (O-phosphorylation) in bacteria remains unclear. Here, we explored the global signaling capacity of the STPKs in Mtb. We generated STPK loss- and gain-of-function strains and measured the resulting O-phosphorylation and transcriptional changes. This deep phosphoproteome shows that O-phosphorylation in Mtb is an underexplored protein modification that affects >70% of the proteome. The substrate-STPK interactions show an extensive interface with the transcriptional machinery, resulting in regulation of gene expression of ~30% of Mtb genes. Mtb O-phosphorylation gives rise to an expansive, distributed, and cooperative network of a complexity that has previously only been associated with eukaryotic phosphosignaling networks.
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