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Structure and chromosomal localization of the aminomethyltransferase gene (AMT)

Genomics (1994-01-01)
K Nanao, G Takada, E Takahashi, N Seki, Y Komatsu, K Okamura-Ikeda, Y Motokawa, K Hayasaka
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.