Force measurements of the disruption of the nascent polypeptide chain from the ribosome by optical tweezers

被引：8

作者：

Katranidis, Alexandros ^{[1
]}

Grange, Wilfried ^{[2
]}

Schlesinger, Ramona ^{[1
]}

Choli-Papadopoulou, Theodora ^{[3
]}

Brueggemann, Dorothea ^{[2
]}

Hegner, Martin ^{[2
]}

Bueldt, Georg ^{[1
]}

机构：

[1] Res Ctr Julich, Inst Complex Syst ICS 5, D-52425 Julich, Germany

[2] Trinity Coll Dublin, Sch Phys, CRANN Naughton Inst, Dublin 2, Ireland

[3] Aristotle Univ Thessaloniki, Sch Chem, Biochem Lab, GR-54006 Thessaloniki, Greece

来源：

FEBS LETTERS | 2011年 / 585卷 / 12期

关键词：

In vitro transcription/translation; Optical tweezers; Ribosome; Single molecule study; SINGLE-MOLECULE FLUORESCENCE; FIREFLY LUCIFERASE; PROTEIN-SYNTHESIS; STRUCTURAL BASIS; AMINO-ACID; TRANSLATION; TIME; EVOLUTION; SELECTION; DYNAMICS;

D O I：

10.1016/j.febslet.2011.04.045

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：

We show that optical tweezers are a valuable tool to study the co-translational folding of a nascent polypeptide chain at the ribosome in real-time. The aim of this study was to demonstrate that a stable and intact population of ribosomes can be tethered to polystyrene beads and that specific hook-ups to the nascent polypeptide chain by dsDNA handles, immobilized on a second bead, can be detected. A rupture force of the nascent chain in the range of 10-50 pN was measured, which demonstrates that the system is anchored to the surface in a stable and specific way. This will allow in numerous future applications to follow protein folding using much lower forces. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：1859 / 1863

页数：5

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