Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

An important 2'-OH group for an RNA-protein interaction.

Y M Hou1, X Zhang, J A Holland

  • 1Department of Biochemistry and Molecular Pharmacology, Thomas Jefferson University, Philadelphia, PA 19107, USA. ya-ming.hou@mail.tju.edu

Nucleic Acids Research
|February 13, 2001
PubMed
Summary

The 2'-OH group at U73 in Escherichia coli tRNA(Cys) acts as a steric sensor, not a hydrogen bond donor, ensuring specific cysteine-tRNA synthetase binding and aminoacylation. This interaction is crucial for high aminoacylation specificity.

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

Observation of Single-Top-Quark Production in Association with a Photon Using the ATLAS Detector.

Physical review letters·2023
Same author

Observation of the γγ→ττ Process in Pb+Pb Collisions and Constraints on the τ-Lepton Anomalous Magnetic Moment with the ATLAS Detector.

Physical review letters·2023
Same author

Strong Constraints on Jet Quenching in Centrality-Dependent p+Pb Collisions at 5.02 TeV from ATLAS.

Physical review letters·2023
Same author

Search for Heavy Neutral Leptons in Decays of W Bosons Using a Dilepton Displaced Vertex in sqrt[s]=13  TeV pp Collisions with the ATLAS Detector.

Physical review letters·2023
Same author

Test of CP Invariance in Higgs Boson Vector-Boson-Fusion Production Using the H→γγ Channel with the ATLAS Detector.

Physical review letters·2023
Same author

Observation of WWW Production in pp Collisions at sqrt[s]=13  TeV with the ATLAS Detector.

Physical review letters·2022

Area of Science:

  • Molecular Biology
  • Biochemistry
  • RNA Structure and Function

Background:

  • The acceptor stem of transfer RNA (tRNA) is critical for aminoacylation specificity.
  • Cysteine-tRNA synthetase (CysRS) exhibits high specificity for its cognate tRNA(Cys).
  • The role of 2 eal-hydroxyl (2 eal-OH) groups in RNA-protein interactions is not fully understood.

Purpose of the Study:

  • To investigate the specific role of 2 eal-OH groups in the acceptor stem of Escherichia coli tRNA(Cys) during interaction with cysteine-tRNA synthetase.
  • To determine whether 2 eal-OH groups are involved in hydrogen bonding or steric recognition.

Main Methods:

  • Synthesis of RNA microhelices mimicking the tRNA(Cys) acceptor stem.
  • Systematic substitution of 2 eal-OH groups with 2 eal-deoxy or 2 eal-O-methyl groups.

Related Experiment Videos

  • Biochemical assays to measure aminoacylation levels.
  • NMR-based structural modeling.

    • Main Results:

    • Substitution of 2 eal-OH groups at most positions had minimal impact on aminoacylation.
    • The 2 eal-deoxy substitution at position U73 did not affect aminoacylation.
    • 2 eal-O-methyl or 2 eal-O-propyl substitutions at U73 significantly decreased aminoacylation.
    • Structural and biochemical data confirmed a steric role for the U73 2 eal-OH group.

    Conclusions:

    • The 2 eal-OH group at position U73 of tRNA(Cys) functions as a steric determinant, not a hydrogen bond donor, in CysRS recognition.
    • This steric interaction is essential for the high aminoacylation specificity of CysRS.
    • The U73 binding site on CysRS is sterically optimized to accommodate the 2 eal-OH group.