The basis of asymmetry in the SecA:SecB complex.
The basis of asymmetry in the SecA:SecB complex.
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DOI:
10.1016/j.jmb.2014.12.008
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发表时间:
2015-02-27
影响因子:
5.6
通讯作者:
Randall, Linda L.
中科院分区:
文献类型:
--
作者:
Suo, Yuying;Hardy, Simon J. S.;Randall, Linda L.
During export in Escherichia coli, SecB, a homotetramer, structurally organized as a dimer of dimers, forms a complex with two protomers of SecA, which is the ATPase that provides energy to transfer a precursor polypeptide through the membrane via the SecYEG translocon. There are two areas of contact on SecB that stabilize the SecA:SecB complex: one, the flat sides of the SecB tetramer and the second, the C-terminal thirteen residues of SecB. These contacts within the complex are distributed asymmetrically. Breaking contact between SecA and the sides of SecB results in release of only one protomer of SecA yielding a complex of stoichiometry SecA1:SecB4. This complex mediates export; however, the coupling of ATP hydrolysis to movements of the precursor through the translocon is much less efficient than the coupling by the SecA2:SecB4 complex. Here we used heterotetrameric species of SecB to understand the source of the asymmetry in the contacts and its role in the functioning of the complex. The model of interactions presented suggests a way that binding between SecA and SecB might decrease the affinity of precursor polypeptides for SecB and facilitate the transfer to SecA.
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影响因子:
5.6
作者:
Crane, Jennine M.;Suo, Yuying;Randall, Linda L.
通讯作者:
Randall, Linda L.
影响因子:
8
作者:
Randall, LL;Topping, TB;Hardy, SJS
通讯作者:
Hardy, SJS
影响因子:
3.2
作者:
Mao, Chunfeng;Hardy, Simon J. S.;Randall, Linda L.
通讯作者:
Randall, Linda L.
影响因子:
2.9
作者:
VANHOLDE, KE;WEISCHET, WO
通讯作者:
WEISCHET, WO
影响因子:
8
作者:
Randall, LL;Crane, JM;Hardy, SJS
通讯作者:
Hardy, SJS