PMID:1325970
| Citation |
Talarico, TL, Ray, PH, Dev, IK, Merrill, BM and Dallas, WS (1992) Cloning, sequence analysis, and overexpression of Escherichia coli folK, the gene coding for 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase. J. Bacteriol. 174:5971-7 |
|---|---|
| Abstract |
The gene coding for the Escherichia coli enzyme 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase has been cloned and sequenced. This gene, designated folK, codes for a protein of 159 amino acids, including an amino-terminal methionine. The protein was overexpressed in E. coli MC4100 by cloning the gene behind the lacUV5 promoter in a high-copy-number plasmid. The enzyme was purified to homogeneity. Amino-terminal analysis of the purified protein showed that the amino-terminal methionine had been removed. The compositional molecular mass (17,945 Da) was identical to the molecular mass determined by mass spectrometry. The enzyme was observed to have a large number of proline residues and migrated anomalously in sodium dodecyl sulfate-polyacrylamide gels, with an apparent molecular mass of 23,000 Da. |
| Links | |
| Keywords |
Amino Acid Sequence; Amino Acids/analysis; Artifacts; Base Sequence; Cloning, Molecular; Diphosphotransferases; Escherichia coli/enzymology; Escherichia coli/genetics; Folic Acid/biosynthesis; Gene Expression; Mass Spectrometry; Molecular Sequence Data; Molecular Weight; Phosphotransferases/biosynthesis; Phosphotransferases/genetics; Phosphotransferases/isolation & purification; Protein Processing, Post-Translational; Sequence Homology, Nucleic Acid |
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