Structure and chromosomal localization of the aminomethyltransferase gene (AMT)
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.
Nanao
K
K
Department of Pediatrics, Akita University School of Medicine, Japan.
Takada
G
G
Takahashi
E
E
Seki
N
N
Komatsu
Y
Y
Okamura-Ikeda
K
K
Motokawa
Y
Y
Hayasaka
K
K
D000592:Amino Acid Metabolism, Inborn Errors / Q000235:genetics*; D050960:Aminomethyltransferase; D001483:Base Sequence; D002874:Chromosome Mapping; D002893:Chromosomes, Human, Pair 3; D005091:Exons; D005796:Genes; D005998:Glycine / Q000097:blood*; D006801:Humans; D019877:Hydroxymethyl and Formyl Transferases; D017404:In Situ Hybridization, Fluorescence; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes; D016133:Polymerase Chain Reaction; D012045:Regulatory Sequences, Nucleic Acid; D014166:Transferases / Q000172:deficiency / Q000235:genetics*
D009097:Multienzyme Complexes; D014166:Transferases; D019877:Hydroxymethyl and Formyl Transferases; D050960:Aminomethyltransferase; D005998:Glycine