The NH2-terminal extension of rat liver arginyl-tRNA synthetase is responsible for its hydrophobic properties

Shouting Huang, Murray P Deutscher

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Rat liver arginyl-tRNA synthetase is found in extracts either as a component (Mr = 72,000) of the multienzyme aminoacyl-tRNA synthetase complex or as a low molecular weight (Mr = 60,000) free protein. The two forms are thought to be identical except for an extra peptide extension at the NH2-terminus of the larger form which is required for its association with the complex, but is unessential for catalytic activity. It has been suggested that interactions among synthetases in the multienzyme complex are mediated by hydrophobic domains on these peptide extensions of the individual proteins. To test this model we have purified to homogeneity the larger form of arginyl-tRNA synthetase and compared its hydrophobicity to that of its low molecular weight counterpart. We show that whereas the smaller protein displays no hydrophobic character, the larger protein demonstrates a high degree of hydrophobicity. No lipid modification was found on the high molecular weight protein indicating that the amino acid sequence itself is responsible for its hydrophobic properties. These findings support the proposed model for synthetase association within the multienzyme complex.

Original languageEnglish
Pages (from-to)702-708
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume180
Issue number2
DOIs
StatePublished - Oct 31 1991
Externally publishedYes

Fingerprint

Arginine-tRNA Ligase
Liver
Rats
Multienzyme Complexes
Molecular Weight
Molecular weight
Ligases
Hydrophobicity
Proteins
Hydrophobic and Hydrophilic Interactions
Amino Acyl-tRNA Synthetases
Peptides
Amino Acid Sequence
Catalyst activity
Lipids
Amino Acids

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

The NH2-terminal extension of rat liver arginyl-tRNA synthetase is responsible for its hydrophobic properties. / Huang, Shouting; Deutscher, Murray P.

In: Biochemical and Biophysical Research Communications, Vol. 180, No. 2, 31.10.1991, p. 702-708.

Research output: Contribution to journalArticle

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