Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Misactivated amino acids translocate at similar rates across surface of a tRNA synthetase

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Nomanbhoy, T. K.
  • Schimmel, Paul

publication date

  • May 2000

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Certain aminoacyl-tRNA synthetases have a second active site that destroys (by hydrolysis) errors of amino acid activation. For example, isoleucyl-tRNA synthetase misactivates valine (to produce valyl adenylate or Val-tRNA(Ile)) at its active site. The misactivated amino acid is then translocated to an editing site located >25 A away. The role of the misactivated amino acid in determining the rate of translocation is not known. Valyl-tRNA synthetase, a close homolog of isoleucyl-tRNA synthetase, misactivates threonine, alpha-aminobutyrate, and cysteine. In this paper, we use a recently developed fluorescence-energy-transfer assay to study translocation of misactivated threonine, alpha-aminobutyrate, and cysteine. Although their rates of misactivation are clearly distinct, their rates of translocation are similar. Thus, the rate of translocation is independent of the nature of the misactivated amino acid. This result suggests that the misactivated amino acid per se has little or no role in directing translocation.

subject areas

  • Amino Acids
  • Aminobutyrates
  • Binding Sites
  • Cloning, Molecular
  • Cysteine
  • Energy Transfer
  • Escherichia coli
  • Isoleucine-tRNA Ligase
  • Kinetics
  • Models, Molecular
  • Open Reading Frames
  • Protein Conformation
  • RNA Editing
  • RNA, Transfer, Val
  • Recombinant Proteins
  • Spectrometry, Fluorescence
  • Threonine
  • Valine-tRNA Ligase
scroll to property group menus

Identity

PubMed Central ID

  • PMC25791

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.090102197

PubMed ID

  • 10792042
scroll to property group menus

Additional Document Info

start page

  • 5119

end page

  • 5122

volume

  • 97

issue

  • 10

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support