A B12-responsive IRES element in human methionine synthase

doi:10.1074/jbc.M501964200

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Papers In Press, published online ahead of print July 28, 2005
J. Biol. Chem, 10.1074/jbc.M501964200
Submitted on February 22, 2005
Revised on July 27, 2005
Accepted on July 28, 2005

A B₁₂-responsive IRES element in human methionine synthase

Sebastian Oltean and Ruma Banerjee

Department of Biochemistry, University of Nebraska, Lincoln, NE 68588-0664

Corresponding Author: rbanerjee1{at}unl.edu

Regulation of homocysteine, a sulfur containing amino acid that is a risk factor for cardiovascular diseases, is poorly understood. Methionine synthase (MS) is a key enzyme that clears intracellular homocysteine and its activity is induced by its cofactor, vitamin B₁₂, at a translational level. In this study, we demonstrate that translation of MS, which has a long and highly structured 5' untranslated region, is initiated from an internal ribosome entry site (IRES), which is modulated by B₁₂. The minimal IRES element spans 71 bases immediately upstream of the initiation codon. Electrophoretic mobility shift analysis reveals the presence of a B₁₂-dependent protein-RNA complex and suggests the possibility that B₁₂ dependent increase of IRES efficiency is mediated via a protein. Modulation of the IRES-dependent translation of an essential gene by the cofactor of the encoded enzyme represents a novel example of a gene-nutrient interaction.

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