Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Human glycyl-tRNA synthetase. Wide divergence of primary structure from bacterial counterpart and species-specific aminoacylation

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

Overview

authors

  • Shiba, K.
  • Schimmel, Paul
  • Motegi, H.
  • Noda, T.

publication date

  • November 1994

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Several class I and class II human tRNA synthetases are clearly related to their bacterial counterparts. We report here the cloning, cDNA sequence, deduced primary structure, and expression in bacteria of a class II human glycyl-tRNA synthetase. While the human sequence aligns well with a Bombyx mori and a Saccharomyces cerevisiae sequence for glycyl-tRNA synthetase, particularly in the region of the class II-defining sequence motifs, it diverges widely from that of the Escherichia coli enzyme. The divergence is so great that from the sequences alone we cannot conclude that the human and E. coli proteins are descended from homologous genes. Moreover, even though the human and E. coli class II alanyl-tRNA synthetases cross-acylate their respective tRNAs, aminoacylations by the recombinant human and E. coli glycyl-tRNA synthetases are restricted to their homologous tRNAs. The species-specific aminoacylations correlate with a nucleotide sequence difference at a location in the acceptor stem that is known to be critical for aminoacylations by the E. coli enzyme. Thus, glycyl-tRNA synthetase may have followed a path of historical development different in at least some respects from that of several other tRNA synthetases.

subject areas

  • Acylation
  • Amines
  • Amino Acid Sequence
  • Animals
  • Bombyx
  • Cells, Cultured
  • Escherichia coli
  • Glycine-tRNA Ligase
  • Humans
  • Molecular Sequence Data
  • Polymerase Chain Reaction
  • Saccharomyces cerevisiae
  • Sequence Homology, Amino Acid
  • Species Specificity
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 7962006
scroll to property group menus

Additional Document Info

start page

  • 30049

end page

  • 30055

volume

  • 269

issue

  • 47

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support