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Cloning and base sequence analysis of a cDNA encoding mouse lung thioether S-methyltransferase
D R Warner1, N M Mozier, J D Pearson
1National Institute of Neurological Disorders and Stroke, Bethesda, MD 20892.
Biochimica Et Biophysica Acta
|January 19, 1995
Summary
Researchers cloned the thioether S-methyltransferase gene, revealing a protein with key methyltransferase motifs. This enzyme shows sequence similarity to other methyltransferases but not thiopurine S-methyltransferase.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- Thioether S-methyltransferase (TSMT) is crucial for methyl group transfer in compounds containing sulfur, selenium, or tellurium.
- Understanding TSMT's structure and function is vital for its role in xenobiotic metabolism and detoxification.
Purpose of the Study:
- To obtain a cDNA clone of mouse thioether S-methyltransferase.
- To analyze the predicted amino acid sequence and identify conserved motifs.
Main Methods:
- Screening of a mouse lung cDNA library using a polymerase chain reaction-generated probe.
- Sequencing of the entire coding and 3'-untranslated regions.
- Bioinformatic analysis of the predicted protein sequence.
Main Results:
- A cDNA clone for TSMT was successfully obtained and sequenced.
- The predicted protein has 264 amino acids and a molecular weight of 29,460 Da.
- TSMT shares sequence identity with nicotinamide N-methyltransferase and phenylethanolamine N-methyltransferase, but not thiopurine S-methyltransferase.
Conclusions:
- The molecular cloning and characterization of TSMT provide a basis for further functional studies.
- TSMT possesses conserved methyltransferase motifs, suggesting a shared catalytic mechanism with other methyltransferases.
- Despite both being mammalian cytosolic sulfur methyltransferases, TSMT and thiopurine S-methyltransferase exhibit distinct sequence identities, indicating divergent evolutionary paths.

