Ligand crowding at a nascent signal sequence

被引:54
作者
Eisner, G
Koch, HG
Beck, K
Brunner, J
Müller, M [1 ]
机构
[1] Univ Freiburg, Inst Biochem & Mol Biol, D-79104 Freiburg, Germany
[2] Univ Freiburg, Fak Biol, D-79104 Freiburg, Germany
[3] ETH, Inst Biochem, CH-8092 Zurich, Switzerland
关键词
L23; nascent polypeptide chains; protein targeting; signal recognition particle; Trigger factor;
D O I
10.1083/jcb.200306069
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
W e have systematically analyzed the molecular environment of the signal sequence of a growing secretory protein from Escherichia coli using a stage- and site-specific cross-linking approach. Immediately after emerging from the ribosome, the signal sequence of pOmpA is accessible to Ffh, the protein component of the bacterial signal recognition particle, and to SecA, but it remains attached to the surface of the ribosome via protein L23. These contacts are lost upon further growth of the nascent chain, which brings the signal sequence into sole proximity to the chaperone Trigger factor (TF). In its absence, nascent pOmpA shows extended contacts with L23, and even long chains interact in these conditions proficiently with Ffh. Our results suggest that upon emergence from the ribosome, the signal sequence of an E. coli secretory protein gradually becomes sequestered by TF. Although TF thereby might control the accessibility of pOmpA`s signal sequence to Ffh and SecA, it does not influence interaction of pOmpA with SecB.
引用
收藏
页码:35 / 44
页数:10
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