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Ribosome structural dynamics during translation (109.2)
Author(s) -
Noller Harry,
Zhou Jie,
Lancaster Laura,
Donohue John,
Guo Zhuojun,
Li Xun
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.109.2
Subject(s) - ribosome , translation (biology) , gtpase , elongation , biophysics , chromosomal translocation , ef tu , protein subunit , chemistry , messenger rna , molecular dynamics , molecular motor , conformational change , computational biology , biology , biochemistry , rna , materials science , gene , computational chemistry , ultimate tensile strength , metallurgy
During each step of elongation of the polypeptide chain, coupled translocation of mRNA and tRNAs through the ribosome is catalyzed by the GTPase elongation factor EF‐G. This complex mechanical process is accompanied by large‐scale structural changes in the ribosome, including intersubunit rotation and rotational movements of the head of the small subunit. The nature of these molecular movements can be pieced together from crystal structures of trapped translocation intermediates. The timing of the different dynamic events can be determined by FRET and other biophysical methods. A detailed description of the molecular mechanism of translocation is emerging from a combination of these different approaches.