Structure and activity of a new form of the glutamate transporter of the nematode Caenorhabditis elegans

Biosci Biotechnol Biochem. 1997 May;61(5):927-9. doi: 10.1271/bbb.61.927.

Abstract

A Caenorhabditis elegans cDNA for a glutamate transporter was cloned and examined in this study. The predicted protein is 11 residues shorter at the N-terminus than Ceglut-1, which we previously reported. The protein, when expressed in Xenopus laevis oocytes, showed much higher glutamate transport activity than Ceglut-1, suggesting that the N-terminal sequence is critical in glutamate transport.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Binding Cassette Transporters / chemistry*
  • ATP-Binding Cassette Transporters / physiology
  • Amino Acid Sequence
  • Amino Acid Transport System X-AG
  • Animals
  • Base Sequence
  • Biological Transport / physiology
  • Caenorhabditis elegans / metabolism*
  • Cloning, Molecular
  • Molecular Sequence Data
  • Oocytes / metabolism
  • Recombinant Proteins / biosynthesis
  • Structure-Activity Relationship
  • Xenopus laevis

Substances

  • ATP-Binding Cassette Transporters
  • Amino Acid Transport System X-AG
  • Recombinant Proteins

Associated data

  • GENBANK/D86741
  • GENBANK/U51998