In vitro induction of H1-H1 histone cross-linking by adenosine diphosphate-ribose polymers.
Biochemistry
; 39(34): 10413-8, 2000 Aug 29.
Article
in En
| MEDLINE
| ID: mdl-10956031
ABSTRACT
It is well-known that H1-H1 interactions are very important for the induction of 30 nm chromatin fiber and that, among all posttranslational modifications, poly(ADP-ribosyl)ation is one of those capable of modifying chromatin structure, mainly through H1 histone. As this protein can undergo both covalent and noncovalent modifications by poly(ADP-ribosyl)ation, our aim was to investigate whether and how ADP-ribose polymers, by themselves, are able to affect the formation of H1-H1 oligomers, which are normally present in a condensed chromatin structure. The results obtained in our in vitro experimental system indicate that ADP-ribose polymers are involved in chromatin decondensation. This conclusion was reached as the result of two different observations (a) H1 histone molecules can be hosted in clusters on ADP-ribose polymers, as shown by their ability to be chemically cross-linked, and (b) H1 histone has a higher affinity for ADP-ribose polymers than for DNA; ADP-ribose polymers compete, in fact, with DNA for H1 histone binding.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Poly Adenosine Diphosphate Ribose
/
Histones
Limits:
Animals
Language:
En
Journal:
Biochemistry
Year:
2000
Document type:
Article
Affiliation country:
Italy