Recombinant cyclophilins lack nuclease activity.
Several single-domain prokaryotic and eukaryotic cyclophilins have been identified as also being unspecific nucleases with a role in DNA degradation during the lytic processes that accompany bacterial cell death and eukaryotic apoptosis. Evidence is provided here that the supposed nuclease activity of human and bacterial recombinant cyclophilins is due to contamination of the proteins by the host Escherichia coli endonuclease and is not an intrinsic property of these proteins.
Manteca
Angel
A
Universidad de Oviedo, Departamento de Biología Funcional, Area de Microbiologia, Julian Claveria s/n, Oviedo 33006, Spain.
Sanchez
Jesus
J
D021983:Cyclophilins / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism*; D004247:DNA / Q000378:metabolism; D004706:Endodeoxyribonucleases / Q000302:isolation & purification / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology* / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000302:isolation & purification / Q000378:metabolism; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism
D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; D004247:DNA; D004706:Endodeoxyribonucleases; D021983:Cyclophilins