Structure and chromosomal localization of the aminomethyltransferase gene (AMT)

Genomics. 1994 Jan 1;19(1):27-30. doi: 10.1006/geno.1994.1007.

Abstract

The gene for human aminomethyltransferase (AMT), also known as the T-protein of the glycine cleavage system, was isolated from a human placental cosmid library and examined by restriction mapping, polymerase chain reaction analysis, and DNA sequencing. The gene is about 6 kb in length and consists of nine exons. The 5'-flanking region of the gene lacks typical TATAA sequence but has a single defined transcription initiation site detected by the primer extension method. Two putative glucocorticoid-responsive elements and a putative thyroid hormone-responsive element are present. The AMT gene was assigned to subband 3p21.2-p21.1 by fluorescence in situ hybridization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Metabolism, Inborn Errors / genetics*
  • Aminomethyltransferase
  • Base Sequence
  • Chromosome Mapping
  • Chromosomes, Human, Pair 3*
  • Exons
  • Genes*
  • Glycine / blood*
  • Humans
  • Hydroxymethyl and Formyl Transferases*
  • In Situ Hybridization, Fluorescence
  • Molecular Sequence Data
  • Multienzyme Complexes
  • Polymerase Chain Reaction
  • Regulatory Sequences, Nucleic Acid
  • Transferases / deficiency
  • Transferases / genetics*

Substances

  • Multienzyme Complexes
  • Transferases
  • Hydroxymethyl and Formyl Transferases
  • Aminomethyltransferase
  • Glycine

Associated data

  • GENBANK/D14681
  • GENBANK/D14682
  • GENBANK/D14684
  • GENBANK/D14685
  • GENBANK/D14686