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- W2040211121 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." @default.
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- W2040211121 date "2000-08-01" @default.
- W2040211121 modified "2023-09-25" @default.
- W2040211121 title "In Vitro Induction of H1−H1 Histone Cross-Linking by Adenosine Diphosphate−Ribose Polymers†" @default.
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- W2040211121 doi "https://doi.org/10.1021/bi992977q" @default.
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