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Human methionine synthase. cDNA cloning, gene localization, and expression

L H Chen¹, M L Liu, H Y Hwang

¹Department of Nutritional Sciences, University of California, Berkeley, California 94720-3104, USA.

The Journal of Biological Chemistry

|February 7, 1997

Summary

Researchers isolated human methionine synthase cDNAs, revealing a 140.3-kDa protein. They identified common genetic variations and mapped the methionine synthase gene to chromosome 1q42.3-43.

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Area of Science:

Biochemistry
Molecular Biology
Genetics

Background:

Methionine synthase (EC 2.1.1.13) is crucial for one-carbon metabolism.
Understanding human methionine synthase is vital for metabolic and genetic research.

Purpose of the Study:

To isolate and characterize human methionine synthase cDNAs.
To analyze the gene's structure, expression, and chromosomal localization.

Main Methods:

cDNA isolation from human liver and HepG2 libraries.
Sequence analysis and protein homology comparisons.
Northern blot analysis for mRNA expression.
In situ hybridization for gene mapping.

Main Results:

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Isolated 7.2 kb human cDNAs encoding a 140.3-kDa methionine synthase protein.

Identified sequence homology with bacterial and nematode homologs, including B12 binding residues.

Detected common polymorphisms, including a D919G modification.

Observed varied mRNA expression levels across human tissues and developmental stages.

Localized the human methionine synthase gene to chromosome 1q42.3-43.

Conclusions:

The study provides a comprehensive characterization of human methionine synthase cDNA.
Genetic variations and tissue-specific expression patterns offer insights into its regulation.
The gene's localization provides a basis for further genetic studies and disease association research.