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.
Conference Article| October 26 2004
Functional ramifications of FRET-detected nascent chain folding far inside the membrane-bound ribosome
A.E. Johnson 1
1Department of Medical Biochemistry and Genetics, Texas A&M University System Health Science Center, 116 Reynolds Medical Bldg., 1114 TAMU, College Station, TX 77843-1114, U.S.A.
2Department of Chemistry and Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, U.S.A.
1To whom correspondence should be addressed at Wehner-Welch Chair, Texas A&M University System Health Science Center (email firstname.lastname@example.org).
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A.E. Johnson; Functional ramifications of FRET-detected nascent chain folding far inside the membrane-bound ribosome. Biochem Soc Trans 1 November 2004; 32 (5): 668–672. doi: https://doi.org/10.1042/BST0320668
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