Depletion of SecDF-YajC causes a decrease in the level of SecG: implication for their functional interaction
Depletion of SecDF-YajC causes a decrease in the level of SecG: implication for their functional interaction
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DOI：
10.1016/s0014-5793(03)00847-0
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发表时间：
2003-08-28
期刊：
影响因子：
3.5
通讯作者：
Tokuda, H
中科院分区：
文献类型：
--
作者：
Kato, Y;Nishiyama, K;Tokuda, H
SecA和包含SecYEG和SecDF-YajC复合物的装置催化蛋白质易位穿过大肠杆菌膜。SecDF-YajC和SecG促进SecA的膜插入，这是蛋白质易位的驱动力。在这里，我们报告说，SecDF-YajC耗尽与SecG耗尽几乎完全抑制蛋白质易位在体内和体外，虽然SecDF-YajC已被认为是不必要的体外易位。在SecDF-YajC耗尽后，膜中SecG的水平降低至约一半，并且当SecDF-YajC表达时恢复至正常水平。SecDF-YajC抑制具有单个半胱氨酸残基的两个SecG分子之间的二硫键形成。这些结果表明SecDF-YajC和SecG之间的功能相互作用。(C)2003年由Elsevier B. V.代表欧洲生物化学学会联合会出版。
SecA and an apparatus comprising SecYEG and SecDF-YajC complexes catalyze protein translocation across the Escherichia coli membrane. SecDF-YajC and SecG facilitate membrane insertion of SecA, which is the driving force for protein translocation. Here we report that SecDF-YajC depletion together with SecG depletion nearly completely inhibits protein translocation both in vivo and in vitro, although SecDF-YajC had been thought to be unnecessary for in vitro translocation. The level of SecG in membranes decreased to about half upon SecDF-YajC depletion and recovered to a normal level when SecDF-YajC was expressed. SecDF-YajC inhibited disulfide bond formation between two SecG molecules possessing a single cysteine residue. These results suggest functional interaction between SecDF-YajC and SecG. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.