Back to Search
Start Over
RPA nucleic acid-binding properties of IFI16-HIN200
- Source :
- Biochimica et biophysica acta. 1784(7-8)
- Publication Year :
- 2008
-
Abstract
- InterFeron-gamma Inducible protein 16 (IFI16) belongs to the interferon inducible HIN200 protein family that contains transcriptional regulators linked to cell cycle regulation and differentiation. All family members contain at most two domains of 200 amino acids, called HIN200, each containing two Oligonucleotide/Oligosaccharide Binding (OB) folds. IFI16 is involved in transcriptional repression and is a component of the DNA repair multi-protein complex known as BASC, which forms after UV-induced DNA damage. In this study, we used fold recognition and biophysical approaches as a tool to infer and validate functions to the HIN200 domain. Since the best template to model IFI16-HIN200 is Replication Protein A (RPA) in complex with single-stranded nucleic acids, we tested six RPA nucleic acid-binding characteristics for IFI16-HIN200. Our results indicate that IFI16-HIN200 is an RPA-like, OB-fold, nucleic acid-binding protein that binds to ssDNA with higher affinity than to dsDNA, recognizes ssDNA in the same orientation as RPA, oligomerizes upon ssDNA binding, wraps and stretches ssDNA, but does not destabilize dsDNA. We finally propose a framework model explaining how the HIN200 domain could prevent ssDNA from re-annealing.
- Subjects :
- Protein family
DNA repair
Biophysics
Plasma protein binding
Biology
Biochemistry
DNA-binding protein
Analytical Chemistry
Biopolymers
Oligosaccharide binding
Fluorescence Resonance Energy Transfer
Humans
Cloning, Molecular
Molecular Biology
Replication protein A
DNA Primers
Base Sequence
Oligonucleotide
Nuclear Proteins
Phosphoproteins
DNA-Binding Proteins
enzymes and coenzymes (carbohydrates)
Nucleic acid
Mutagenesis, Site-Directed
Protein Binding
Subjects
Details
- ISSN :
- 00063002
- Volume :
- 1784
- Issue :
- 7-8
- Database :
- OpenAIRE
- Journal :
- Biochimica et biophysica acta
- Accession number :
- edsair.doi.dedup.....57e7fba5793fee4b4e294909ad1ccb50