Yellow Lupine Cyclophilin Interacts with Nucleic Acids

Title: Yellow Lupine Cyclophilin Interacts with Nucleic Acids

Volume: 15 Issue: 7

Author(s): Katarzyna Nuc, Krzysztof Lesniewicz, Przemyslaw Nuc and Ryszard Slomski

Affiliation:

Keywords: Cyclophilin, Isomerase, Protein expression, DNA-protein interaction

Abstract: To investigate properties of yellow lupine cytosolic cyclophilin, an expression vector pET15CYP was constructed. The CyP cDNA (GenBank accession no.Y16088) reveals an open reading frame of 172 amino acids with the conserved tryptophan residue at position 128 and an insertion of seven amino acids spanning positions 48-54. Yellow lupine cyclophilin, purified after expression in E. coli cells, exhibits peptidyl-prolyl cis/trans isomerase activity when assayed with a synthetic oligopeptide. We have demonstrated that the recombinant cyclophilin is able to interact with nucleic acids, both single and double stranded DNA fragments as well as RNA.

Cite this article as:

Nuc Katarzyna, Lesniewicz Krzysztof, Nuc Przemyslaw and Slomski Ryszard, Yellow Lupine Cyclophilin Interacts with Nucleic Acids, Protein & Peptide Letters 2008; 15(7) . https://dx.doi.org/10.2174/092986608785133726