Sequence and expression of the gene forN10-formyltetrahydrofolate synthetase fromClostridium cylindrosporum
- 1 February 1993
- journal article
- research article
- Published by Wiley in Protein Science
- Vol. 2 (2) , 197-205
- https://doi.org/10.1002/pro.5560020208
Abstract
Sau3 A and Hind III restriction fragments of Clostridium cylindrosporum genomic DNA were used to isolate clones containing 80% of the N10‐H4folate synthetase gene in a 5′ fragment and the remaining 20% of the gene in the 3′ fragment. These fragments were joined at a common SnaB I restriction site and expressed in Escherichia coli at a level equivalent to what is normally found in C. cylindrosporum. Sequence comparisons show a large degree of homology with genes from two other clostridial species, including a thermophile. Certain conserved sequences found in the three clostridial proteins and in the N10‐H4folate synthetase portion of eukaryotic Cl‐H4folate synthases may represent consensus sequences for nucleotide and H4folate binding.Keywords
Funding Information
- National Institutes of Health (DK 07140)
- University of Kansas Graduate Research Fund
This publication has 40 references indexed in Scilit:
- Primary structure of the thermostable formyltetrahydrofolate synthetase from Clostridium thermoaceticum. [Erratum to document cited in CA113(3):20097s]Biochemistry, 1992
- Primary structure of the thermostable formyltetrahydrofolate synthetase from Clostridium thermoaceticumBiochemistry, 1990
- Formation and utilization of formyl phosphate by N10-formyltetrahydrofolate synthetase: evidence for formyl phosphate as an intermediate in the reactionBiochemistry, 1989
- A model of the nucleotide‐binding site in tubulinFEBS Letters, 1987
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- Formyl-methenyl-methylenetetrahydrofolate synthetase (combined): Correlation of enzymic activities with limited proteolytic degradation of the protein from yeastBiochemical and Biophysical Research Communications, 1977
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Observations on the monovalent cation requirements of formyltetrahydrofolate synthetaseBiochemical and Biophysical Research Communications, 1968
- The association-dissociation of formyltetrahydrofolate synthetase and its relation to monovalent cation activation of catalytic activityBiochemical and Biophysical Research Communications, 1967