The major chromatin protein histone H1 binds preferentially to cis-platinum-damaged DNA
AUTOR(ES)
Yaneva, Julia
FONTE
The National Academy of Sciences of the USA
RESUMO
Both cis-diamminedichloroplatinum(II) (cisplatin or cis-DDP) and trans-diamminedichloroplatinum(II) form covalent adducts with DNA. However, only the cis isomer is a potent anticancer agent. It has been postulated that the selective action of cis-DDP occurs through specific binding of nuclear proteins to cis-DDP-damaged DNA sites and that binding blocks DNA repair. We find that a very abundant nuclear protein, the linker histone H1, binds much more strongly to cis-platinated DNA than to trans-platinated or unmodified DNA. In competition experiments, H1 is shown to bind much more strongly than HMG1, which had been previously considered a major candidate for such binding in vivo.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=28325Documentos Relacionados
- Histone H1 preferentially binds to superhelical DNA molecules of higher compaction.
- Histone H1 deposition and histone-DNA interactions in replicating chromatin.
- The repressor MDBP-2 is a member of the histone H1 family that binds preferentially in vitro and in vivo to methylated nonspecific DNA sequences.
- Binding of phosphorylated histone H1 to DNA.
- Influence of histone H1 on the in vitro replication of DNA and chromatin.
