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Heterogeneity of single molecule FRET signals reveals multiple active ribosome subpopulations
Author(s) -
Wang Yuhong,
Xiao Ming,
Li Yue
Publication year - 2014
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24308
Subject(s) - förster resonance energy transfer , single molecule fret , ribosome , transfer rna , biology , computational biology , translation (biology) , single molecule experiment , function (biology) , biophysics , ribosome profiling , molecule , biological system , fluorescence , chemistry , microbiology and biotechnology , rna , physics , genetics , messenger rna , gene , organic chemistry , quantum mechanics
Single molecule methods have revealed that heterogeneity is common in biological systems. However, interpretations of the complex signals are challenging. By tracking the fluorescence resonance energy transfer (FRET) signals between the A‐site tRNA and L27 protein in single ribosomes, we attempt to develop a qualitative method to subtract the inherent patterns of the heterogeneous single molecule FRET data. Seven ribosome subpopulations are identified using this method and spontaneous exchanges among these subpopulations are observed. All of the pretranslocation subpopulations are competent in real‐time translocation, but via distinguished pathways. These observations suggest that the ribosome may function through multiple reaction pathways. Proteins 2014; 82:1–9. © 2013 Wiley Periodicals, Inc.