Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Related Experiment Videos

Structure-specific tRNA determinants for editing a mischarged amino acid.

Kirk Beebe¹, Eve Merriman, Paul Schimmel

¹Department of Molecular Biology and Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA.

The Journal of Biological Chemistry

|September 2, 2003

Summary

Alanyl-tRNA synthetase editing depends on the tRNA

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Conserved shifts in sperm small non-coding RNA profiles during mouse and human aging.

The EMBO journal·2026

Same author

Real-World Validation of the Purity Independent Subtyping of Tumors Classifier for Informing Therapy Selection in Pancreatic Ductal Adenocarcinoma.

JCO precision oncology·2025

Same author

A phase 1/2a dose-finding study and biomarker assessment of oral lisavanbulin in patients with high-grade glioma or glioblastoma.

Cell reports. Medicine·2025

Same author

A human histidyl-tRNA synthetase splice variant therapeutic targets NRP2 to resolve lung inflammation and fibrosis.

Science translational medicine·2025

Same author

Rheumatoid arthritis associated cytokines and therapeutics modulate immune checkpoint receptor expression on T cells.

Frontiers in immunology·2025

Same author

Metabolic regulation of mRNA splicing.

Trends in cell biology·2024

Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Alanyl-tRNA synthetase (AlaRS) aminoacylates tRNAAla and RNA minihelices.
AlaRS possesses a C-terminal domain for editing mischarged tRNAAla.
RNA minihelices lack editing capabilities compared to full-length tRNAAla.

Purpose of the Study:

Investigate structural determinants for AlaRS editing.
Differentiate editing mechanisms between minihelixAla and tRNAAla.
Understand the role of tRNA structure in preventing aminoacylation errors.

Main Methods:

Constructed chimeric tRNAs with modified acceptor stems.
Assessed mischarging and editing of chimeric tRNAs by AlaRS.
Compared editing efficiency of minihelixAla, tRNAAla, and chimeric tRNAs.

Related Experiment Videos

Main Results:

Mischarged minihelixAla could not be edited, even with an added domain.
Chimeric tRNAs, despite sequence variations, were effectively edited by AlaRS.
The acceptor stem alone lacked editing determinants, but the continuous two-domain structure was crucial.

Conclusions:

The covalently continuous, two-domain L-shaped tRNA structure, not specific sequences, is a key determinant for AlaRS editing.
Structure-specific determinants for editing provide a selective pressure to maintain the canonical tRNA structure.
Preventing aminoacylation errors is vital for cellular growth and function.