Third and Final Technical Report for F49620-92-0232-DEF (San Francisco State University).
Abstract
Cellular proteins extracted from normal and cancer cells bind poly(ADP-ribose) polymerase on nitro-cellulose membrane transblots. Histones at 1 rng/ml concentration completely prevent the binding of poly(ADP-ribose) polymerase to cellular proteins, indicating that the binding of histones to poly(ADP-ribose) polymerase sites competitively blocks the association of poly (ADP-ribose) polymerase to proteins other than histones. The direct binding of poly(ADP-ribos polymerase to histones is shown by crosslinking with glutaraldehyde. The C-terminal basic histone Hi tail binds to the basic polypeptide domain of poly(ADP-ribose) polymerase. The basic domain present in the N-terminal part of core histones is the probable common structural feature of all core histones that accounts for their binding to poly(ADP-ribose) polymerase. Two polypeptide domains of poly(ADP-ribose) polymerase were identified, by way of CNBr fragments, to bind histones.
Document Details
- Document Type
- Technical Report
- Publication Date
- Apr 29, 1995
- Accession Number
- ADA294362
Entities
People
- Ernest Kun
Organizations
- San Francisco State University