Functional ramifications of FRET-detected nascent chain folding far inside the membrane-bound ribosome

被引:13
作者
Johnson, AE
机构
[1] Texas A&M Univ, Syst Hlth Sci Ctr, Dept Med Biochem & Genet, College Stn, TX 77843 USA
[2] Texas A&M Univ, Dept Chem, College Stn, TX 77843 USA
[3] Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA
关键词
endoplasmic reticulum membrane; fluorescence spectroscopy; fluorescence resonance energy transfer (FRET); nascent membrane protein; ribosome; translocon;
D O I
10.1042/BST0320668
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
During protein biosynthesis, nascent protein chains are directed along a long narrow tunnel that spans the large ribosomal subunit. It has recently become clear that this structural feature has evolved to effect regulatory control over aspects of protein synthesis and protein trafficking. Since this control is nascent chain-specific, ribosomal components that form the tunnel must be involved in recognizing selected nascent proteins as they pass by. The present study focuses on one such situation in which nascent secretory proteins and membrane proteins are distinguished by the ribosome-induced folding of the latter's hydrophobic transmembrane sequence far inside the ribosomal tunnel and close to the peptidyltransferase centre.
引用
收藏
页码:668 / 672
页数:5
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