Recombinant Cyclophilins Lack Nuclease Activity
نویسندگان
چکیده
منابع مشابه
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 ho...
متن کاملCyclophilins
Cyclophilins constitute a subgroup of large family of proteins called immunophilins, which also include FKBPs and Parvulins. They are remarkably conserved in all genera, highlighting their pivotal role in important cellular processes. Most cyclophilins display PPIase enzymatic activity, multiplicity, diverse cellular locations and active role in protein folding which render them to be included ...
متن کاملSERCA2b activity is regulated by cyclophilins in human platelets.
OBJECTIVE The role of cyclophilins (chaperones that are widely expressed in different cell types, including human platelets) was explored in sarcoendoplasmic calcium (Ca(2+)) adenosine triphosphatase (SERCA) activity. METHODS AND RESULTS Cyclophilin inhibition by cyclosporin A (CsA) evoked a time- and concentration-dependent reduction of Ca(2+) uptake by SERCA2b. However, other Ca(2+)-adenosi...
متن کاملA site-targeted recombinant nuclease probe of DNA structure.
A genetically engineered lac repressor/T7 endonuclease hybrid protein shows repressor-like binding toward restriction fragments carrying the lac operator. In addition, fragments carrying the operator near a particular pBR322 sequence are cleaved into specific products. Cleavage occurs at precise positions within that sequence, is independent of the orientation of the operator, is inhibited by i...
متن کاملReconstitution of human excision nuclease with recombinant XPF-ERCC1 complex.
The human XPF-ERCC1 protein complex is one of several factors known to be required for general nucleotide excision repair. Genetic data indicate that both proteins of this complex are necessary for the repair of interstrand cross-links, perhaps via recombination. To determine whether XPF-ERCC1 completes a set of six proteins that are sufficient to carry out excision repair, the human XPF and ER...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 2004
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.186.18.6325-6326.2004