TY - JOUR
T1 - Human histamine N-methyltransferase gene
T2 - Structural characterization and chromosomal localization
AU - Aksoy, Saime
AU - Raftogianis, Rebecca
AU - Weinshilboum, Richard
N1 - Funding Information:
We thank Luanne Wussow for her assistance with the preparation of this manuscript. Supported in part by NIH grants RO1 GM 28157 (RW) and RO1 GM 35720 (RW). The GenBank accession numbers for the nucleotide sequences listed in Figure 2 are U44106, U44107, U44108, U44109, U44110 and U44111.
PY - 1996/2/15
Y1 - 1996/2/15
N2 - Histamine N-methyltransferase (HNMT) catalyzes the N(τ)-methylation of histamine. The level of HNMT activity in human red blood cells is controlled by a common genetic polymorphism. We previously cloned and expressed a cDNA for human kidney HNMT, and we have now determined the structural organization of the human HNMT gene as a step toward studies of the genetic regulation of levels of HNMT activity in human tissue. Structural characterization of the HNMT gene was performed by use of a polymerase chain reaction (PCR)-based strategy. The gene was approximately 34 kb in length and contained 6 exons. All exon-intron splice junction sequences conformed to the 'GT-AG' rule. The longest transcript isolated after 5'-rapid amplification of cDNA ends indicated that transcription initiation occurred 252 nucleotides 5'-upstream from the cDNA translation initiation codon. HNMT mapped to human chromosome 2. Structural characterization of the gene for HNMT will make it possible to study molecular generic mechanisms involved in the regulation of this important enzyme in humans.
AB - Histamine N-methyltransferase (HNMT) catalyzes the N(τ)-methylation of histamine. The level of HNMT activity in human red blood cells is controlled by a common genetic polymorphism. We previously cloned and expressed a cDNA for human kidney HNMT, and we have now determined the structural organization of the human HNMT gene as a step toward studies of the genetic regulation of levels of HNMT activity in human tissue. Structural characterization of the HNMT gene was performed by use of a polymerase chain reaction (PCR)-based strategy. The gene was approximately 34 kb in length and contained 6 exons. All exon-intron splice junction sequences conformed to the 'GT-AG' rule. The longest transcript isolated after 5'-rapid amplification of cDNA ends indicated that transcription initiation occurred 252 nucleotides 5'-upstream from the cDNA translation initiation codon. HNMT mapped to human chromosome 2. Structural characterization of the gene for HNMT will make it possible to study molecular generic mechanisms involved in the regulation of this important enzyme in humans.
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U2 - 10.1006/bbrc.1996.0271
DO - 10.1006/bbrc.1996.0271
M3 - Article
C2 - 8605025
AN - SCOPUS:0029875216
SN - 0006-291X
VL - 219
SP - 548
EP - 554
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -