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Maintenance of protein synthesis reading frame by EF-P and m¹G37-tRNA

Slippery mRNA sequences CC[C/U]-[C/U] are prone to +1 frameshift (+1FS) errors during mRNA translation. Here, the authors show that +1FS errors occur predominantly when CC[C/U]-[C/U] are placed at the second sense codon, and that error suppression requires m¹G37-tRNA and the translation factor EF-P.

Howard B. Gamper
Isao Masuda
Ya-Ming Hou
Research26 May 2015
Nature Communications

Volume: 6, P: 1-13
An RNA modification prevents extended codon-anticodon interactions from facilitating +1 frameshifting

tRNAs contain many chemical modifications that regulate their function. Integrating smFRET and cryo-EM approaches, this work demonstrates that m¹G37 in tRNA^ProL stabilizes its conformation in the ribosomal P site in a manner that suppresses mRNA frameshifting and ensures translation fidelity.

Evelyn M. Kimbrough
Ha An Nguyen
Christine M. Dunham
ResearchOpen Access11 Aug 2025
Nature Communications

Volume: 16, P: 1-13
Genome-wide profiling of tRNA modifications by Induro-tRNAseq reveals coordinated changes

Here the authors report genome-wide profiling of tRNA modifications using Induro-tRNAseq and uncover coordinated changes across cell types and tissues that underlie the basis of protein homeostasis.

Yuko Nakano
Howard Gamper
Ya-Ming Hou
ResearchOpen Access26 Jan 2025
Nature Communications

Volume: 16, P: 1-19
Insights into genome recoding from the mechanism of a classic +1-frameshifting tRNA

Genome recoding with quadruplet codons requires a +1-frameshift-suppressor tRNA able to insert an amino acid at quadruplet codons of interest. Here the authors identify the mechanisms resulting in +1 frameshifting and the steps of the elongation cycle in which it occurs.

Howard Gamper
Haixing Li
Ya-Ming Hou
ResearchOpen Access12 Jan 2021
Nature Communications

Volume: 12, P: 1-18
Author Correction: The selective tRNA aminoacylation mechanism based on a single G•U pair

Masahiro Naganuma
Shun-ichi Sekine
Shigeyuki Yokoyama
Amendments and Corrections20 Nov 2018
Nature

Volume: 564, P: E37
Post-transcriptional methylation of mitochondrial-tRNA differentially contributes to mitochondrial pathology

Here the authors show that the m¹G9 post-transcriptional methylation differentially regulates the stability of the native and the MELAS variants of human mt-Leu(UAA) tRNA, contributing to mitochondrial pathology.

Sunita Maharjan
Howard Gamper
Ya-Ming Hou
ResearchOpen Access18 Oct 2024
Nature Communications

Volume: 15, P: 1-17
Semi-quantitative detection of pseudouridine modifications and type I/II hypermodifications in human mRNAs using direct long-read sequencing

Pseudouridine (psi) is an RNA modification that can affect its physiology, including increased half-life. Here the authors identify sites of psi modification in the human transcriptome using direct RNA sequencing and provide a “ground truth” list of psi sites, sites of high psi occupancy, and transcripts that may be modified at multiple sites.

Sepideh Tavakoli
Mohammad Nabizadeh
Sara H. Rouhanifard
ResearchOpen Access19 Jan 2023
Nature Communications

Volume: 14, P: 1-12
Nanopore signal deviations from pseudouridine modifications in RNA are sequence-specific: quantification requires dedicated synthetic controls

Amr Makhamreh
Sepideh Tavakoli
Meni Wanunu
ResearchOpen Access28 Sept 2024
Scientific Reports

Volume: 14, P: 1-13
Time-resolved cryo-EM visualizes ribosomal translocation with EF-G and GTP

EF-G drives ribosomal translocation along mRNA. Time-resolved cryo-EM captured translocation with EF-G•GTP—without inhibitors—revealing how EF-G uses ribosome fluctuations to drive translocation and GTP hydrolysis to leave at the right moment.

Christine E. Carbone
Anna B. Loveland
Andrei A. Korostelev
ResearchOpen Access13 Dec 2021
Nature Communications

Volume: 12, P: 1-13
Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation

Translational frameshifting is a mechanism that expands the coding capabilities of mRNA. Here, structures of 70S ribosome complexes with GTPase elongation factor G (EF-G), a +1-frameshifting-prone mRNA and tRNAs reveal the cooperation between the ribosome and EF-G to induce +1 frameshifting during the translocation step.

Gabriel Demo
Howard B. Gamper
Andrei A. Korostelev
ResearchOpen Access30 Jul 2021
Nature Communications

Volume: 12, P: 1-12
Interplay between an ATP-binding cassette F protein and the ribosome from Mycobacterium tuberculosis

The authors present structures of the MtbEttA protein bound to or free of the ribosome from Mycobacterium tuberculosis under different nucleotide states, which provide insights into the mechanism of translational regulation by EttA-like proteins.

Zhicheng Cui
Xiaojun Li
Junjie Zhang
ResearchOpen Access21 Jan 2022
Nature Communications

Volume: 13, P: 1-12
Potential for interdependent development of tRNA determinants for aminoacylation and ribosome decoding

Aminoacyl-transfer RNA synthetases are conserved between bacteria and eukaryotes; however, bacterial enzymes cannot acylate eukaryote tRNAs. Now, fusion of a human and bacterial enzyme is shown to overcome the species barrier and confer tRNA specificity during both codon selection and proofreading on the ribosome.

Cuiping Liu
Howard Gamper
Ya-Ming Hou
Research31 May 2011
Nature Communications

Volume: 2, P: 1-8
The selective tRNA aminoacylation mechanism based on a single G•U pair

X-ray crystal structures of a tRNA synthetase bound to wild-type and mutant alanine tRNAs reveal the structural basis for selectivity.

Masahiro Naganuma
Shun-ichi Sekine
Shigeyuki Yokoyama
Research11 Jun 2014
Nature

Volume: 510, P: 507-511
The Episodic Memory System: Neurocircuitry and Disorders

Bradford C Dickerson
Howard Eichenbaum
Reviews23 Sept 2009
Neuropsychopharmacology

Volume: 35, P: 86-104

Search

Maintenance of protein synthesis reading frame by EF-P and m¹G37-tRNA

An RNA modification prevents extended codon-anticodon interactions from facilitating +1 frameshifting

Genome-wide profiling of tRNA modifications by Induro-tRNAseq reveals coordinated changes

Insights into genome recoding from the mechanism of a classic +1-frameshifting tRNA

Author Correction: The selective tRNA aminoacylation mechanism based on a single G•U pair

Post-transcriptional methylation of mitochondrial-tRNA differentially contributes to mitochondrial pathology

Semi-quantitative detection of pseudouridine modifications and type I/II hypermodifications in human mRNAs using direct long-read sequencing

Nanopore signal deviations from pseudouridine modifications in RNA are sequence-specific: quantification requires dedicated synthetic controls

Time-resolved cryo-EM visualizes ribosomal translocation with EF-G and GTP

Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation

Interplay between an ATP-binding cassette F protein and the ribosome from Mycobacterium tuberculosis

Potential for interdependent development of tRNA determinants for aminoacylation and ribosome decoding

The selective tRNA aminoacylation mechanism based on a single G•U pair

The Episodic Memory System: Neurocircuitry and Disorders

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