EF4 disengages the peptidyl-tRNA CCA end and facilitates back-translocation on the 70S ribosome (Q87155525)

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6 March 2020

title

EF4 disengages the peptidyl-tRNA CCA end and facilitates back-translocation on the 70S ribosome (English)

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2

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Ning Gao

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author name string

Dejiu Zhang

1

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Guangqiao Liu

3

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Guangtao Song

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Jiejian Luo

5

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Yi Shi

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Erchao Cheng

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Shan Wu

8

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Taijiao Jiang

9

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Jizhong Lou

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Yan Qin

12

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publication date

25 January 2016

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Nature Structural & Molecular Biology

6 March 2020

published in

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volume

23

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issue

2

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page(s)

125-131

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EF-G catalyzes tRNA translocation by disrupting interactions between decoding center and codon-anticodon duplex

6 March 2020

cites work

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The highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosome

31 March 2020

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Interrupted catalysis: the EF4 (LepA) effect on back-translocation

31 March 2020

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The conserved protein EF4 (LepA) modulates the elongation cycle of protein synthesis

31 March 2020

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The structure of LepA, the ribosomal back translocase

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EF-G and EF4: translocation and back-translocation on the bacterial ribosome.

31 March 2020

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The paradox of elongation factor 4: highly conserved, yet of no physiological significance?

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A new tRNA intermediate revealed on the ribosome during EF4-mediated back-translocation

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Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome

31 March 2020

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Structure of the 70S ribosome complexed with mRNA and tRNA

31 March 2020

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Identification of two structural elements important for ribosome-dependent GTPase activity of elongation factor 4 (EF4/LepA).

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EF4 knockout E. coli cells exhibit lower levels of cellular biosynthesis under acidic stress

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Elongation factor 4 (EF4/LepA) accelerates protein synthesis at increased Mg2 concentrations

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A conserved proline switch on the ribosome facilitates the recruitment and binding of trGTPases

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Common chaperone activity in the G-domain of trGTPase protects L11-L12 interaction on the ribosome

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https://pubmed.ncbi.nlm.nih.gov/26809121

31 March 2020

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12 December 2020

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