A genetically incorporated crosslinker reveals chaperone cooperation in acid resistance
A genetically incorporated crosslinker reveals chaperone cooperation in acid resistance
复制标题
基因整合的交联剂揭示了耐酸性中的分子伴侣合作。
DOI：
10.1038/nchembio.644
复制
发表时间：
2011-10-01
影响因子：
14.8
通讯作者：
Chen, Peng R.
中科院分区：
文献类型：
--
作者：
Zhang, Meng;Lin, Shixian;Chen, Peng R.
酸伴侣是维持肠道病原体在极酸性哺乳动物胃（pH 1-3）中存活的蛋白质稳态的必要因素。这些伴侣蛋白的客户蛋白在很大程度上仍然是未知的，主要是因为在低pH条件下确定蛋白质-蛋白质相互作用非常困难。我们开发了一种遗传编码的高效蛋白质光交联探针，使我们能够在大肠杆菌周质中分析主要酸保护分子伴侣HdeA的体内底物。在鉴定的HdeA客户蛋白中，最初发现周质伴侣DegP和SurA在低pH下被HdeA保护，但它们随后促进了其他客户蛋白的HdeA介导的酸恢复。这种独特的，ATP-独立的伴侣在ATP-剥夺E合作。大肠杆菌周质可以支持肠细菌的耐酸性。交联剂在揭示任何给定蛋白质的生理相互作用伴侣以及它们在正常和应激条件下的功能方面将是有价值的。
Acid chaperones are essential factors in preserving the protein homeostasis for enteric pathogens to survive in the extremely acidic mammalian stomach (pH 1–3). The client proteins of these chaperones remain largely unknown, primarily because of the exceeding difficulty of determining protein-protein interactions under low-pH conditions. We developed a genetically encoded, highly efficient protein photocrosslinking probe, which enabled us to profile thein vivosubstrates of a major acid-protection chaperone, HdeA, inEscherichia coliperiplasm. Among the identified HdeA client proteins, the periplasmic chaperones DegP and SurA were initially found to be protected by HdeA at a low pH, but they subsequently facilitated the HdeA-mediated acid recovery of other client proteins. This unique, ATP-independent chaperone cooperation in the ATP-deprivedE. coliperiplasm may support the acid resistance of enteric bacteria. The crosslinker would be valuable in unveiling the physiological interaction partners of any given protein and thus their functions under normal and stress conditions.