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Identification of protein-arginine N-methyltransferase as 10-formyltetrahydrofolate dehydrogenase.

Authors
Kim, S; Park, GH; Joo, WA; Paik, WK; Cook, RJ; Williams, KR
Citation
The Journal of biological chemistry, 273(42):27374-27382, 1998
Journal Title
The Journal of biological chemistry
ISSN
0021-92581083-351X
Abstract
S-Adenosylmethionine:protein-arginine N-methyltransferase (EC 2.1.1. 23; protein methylase I) transfers the methyl group of S-adenosyl-L-methionine to an arginine residue of a protein substrate. The homogeneous liver protein methylase I was subjected to tryptic digestion followed by reverse phase high performance liquid chromatography (HPLC) separation and either "on-line" mass spectrometric fragmentation or "off-line" Edman sequencing of selected fractions. Data base searching of both the mass spectrometric and Edman sequencing data from several peptides identified the protein methylase as 10-formyltetrahydrofolate dehydrogenase (EC 1.5.1.6; Cook, R. J., Lloyd, R. S., and Wagner, C. (1991) J. Biol. Chem. 266, 4965-4973; Swiss accession number). This identification was confirmed by comparative HPLC tryptic peptide mapping and affinity chromatography of the methylase on the 5-formyltetrahydrofolate-Sepharose affinity gel used to purify the dehydrogenase. The purified rat liver methylase had approximately 33% of the 10-formyltetrahydrofolate dehydrogenase and 36% of the aldehyde dehydrogenase activity as compared with the recombinant dehydrogenase, which also had protein methylase I activity. Polyclonal antibodies against recombinant dehydrogenase reacted with protein methylase I purified either by polyacrylamide gel electrophoresis or 5-formyltetrahydrofolate affinity chromatography. In each instance there was only a single immunoreactive band at a molecular weight of approximately 106,000. Together, these results confirm the co-identity of protein-arginine methyltransferase and 10-formyltetrahydrofolate dehydrogenase.
MeSH terms
Amino Acid SequenceAnimalsBlotting, WesternChromatography, AffinityChromatography, High Pressure LiquidGas Chromatography-Mass SpectrometryLeucovorin/chemistryLiver/enzymologyMolecular Sequence DataOxidoreductases Acting on CH-NH Group Donors/*chemistry/genetics/immunology/metabolismPeptide MappingProtein-Arginine N-Methyltransferases/*chemistry/genetics/immunology/metabolismRatsRecombinant Proteins/metabolismSepharose/chemistrySequence Analysis
PMID
9765265
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Journal Papers > School of Medicine / Graduate School of Medicine > Biochemistry & Molecular Biology
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