Bacterial protein translocation requires only one copy of the SecY complex in vivo.
Bacterial protein translocation requires only one copy of the SecY complex in vivo.
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DOI:
10.1083/jcb.201205140
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发表时间:
2012-09-03
期刊:
影响因子:
--
通讯作者:
Rapoport TA
中科院分区:
文献类型:
--
作者:
Park E;Rapoport TA
In vivo probing of the oligomeric state of SecY during co- and post-translational translocation reveals that oligomerization is not required for this process. The transport of proteins across the plasma membrane in bacteria requires a channel formed from the SecY complex, which cooperates with either a translating ribosome in cotranslational translocation or the SecA ATPase in post-translational translocation. Whether translocation requires oligomers of the SecY complex is an important but controversial issue: it determines channel size, how the permeation of small molecules is prevented, and how the channel interacts with the ribosome and SecA. Here, we probe in vivo the oligomeric state of SecY by cross-linking, using defined co- and post-translational translocation intermediates in intact Escherichia coli cells. We show that nontranslocating SecY associated transiently through different interaction surfaces with other SecY molecules inside the membrane. These interactions were significantly reduced when a translocating polypeptide inserted into the SecY channel co- or post-translationally. Mutations that abolish the interaction between SecY molecules still supported viability of E. coli. These results show that a single SecY molecule is sufficient for protein translocation.
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DOI:
10.1083/jcb.200412019
发表时间:
2005-04-25
期刊:
The Journal of cell biology
影响因子:
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作者:
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DOI:
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影响因子:
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作者:
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DOI:
10.1074/jbc.m110.175638
发表时间:
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期刊:
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影响因子:
--
作者:
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通讯作者:
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影响因子:
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作者:
Park, Eunyong;Rapoport, Tom A.
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