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

Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.

S Cusack1, M Härtlein, R Leberman

  • 1European Molecular Biology Laboratory, Grenoble, France.

Nucleic Acids Research
|July 11, 1991
PubMed
Summary

Class 2 aminoacyl-tRNA synthetases share conserved sequence motifs, enabling their classification into subclasses. Structural analysis reveals motif functions and evolutionary relationships, suggesting domain additions during evolution.

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

A Study of the Patients Admitted to the Clinical Decision Unit over One Year.

Irish medical journal·2016
Same author

Dynamic footprint of sequestration in the molecular fluctuations of osteopontin.

Journal of the Royal Society, Interface·2015
Same author

Diet-microbiota-health interactions in older subjects: implications for healthy aging.

Interdisciplinary topics in gerontology·2014
Same author

[Hydronephrosis after suburethral sling implantation: diagnosis and operative management in men].

Der Urologe. Ausg. A·2013
Same author

Helicopter winchmens' experiences with pain management in challenging environments.

Irish medical journal·2013
Same author

Dynamical coupling of intrinsically disordered proteins and their hydration water: comparison with folded soluble and membrane proteins.

Biophysical journal·2012

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Class 2 aminoacyl-tRNA synthetases are essential enzymes involved in protein synthesis.
  • These enzymes are characterized by three conserved sequence motifs: motif 1, motif 2, and motif 3.

Purpose of the Study:

  • To examine the structural and evolutionary relatedness of ten Class 2 aminoacyl-tRNA synthetases.
  • To investigate the roles of conserved sequence motifs in enzyme structure and function.

Main Methods:

  • Sequence alignments of primary sequences from prokaryotic and eukaryotic sources.
  • Analysis of the three-dimensional structure of seryl-tRNA synthetase from E. coli.

Main Results:

  • Motif 1 is part of the dimer interface, while motifs 2 and 3 are in the putative active site of seryl-tRNA synthetase.

Related Experiment Videos

  • Class 2 enzymes can be subdivided into class 2a (proline, threonine, histidine, serine) and class 2b (aspartic acid, asparagine, lysine) based on characteristic sequence motifs.
  • Tetrameric enzymes (glycine, phenylalanine) share features with class 2b, while alanyl-tRNA synthetase shows only motif 3 and possibly motif 2.
  • Sequence alignments predict structural similarities in catalytic domains and identify key residues for ATP and amino acid binding.

    • Conclusions:

    • The catalytic domain of Class 2 synthetases resembles the antiparallel domain of seryl-tRNA synthetase.
    • N-terminal and C-terminal extensions likely represent tRNA binding domains added later in evolution.