Linker histones do not interact with DNA containing a single interstrand cross-link created by cisplatin.
During our earlier investigations we have observed a prominent preference of the linker histone H1 for binding to a cis-platinated DNA (a synthetic fragment with global type of platination in respect to targets for cisplatin) comparing with unmodified and trans-Pt-modified DNA. In the present work we report our recent experimental results on the binding of the linker histones H1 and H5 to a cisplatin-modified synthetic DNA fragment containing a single nucleotide target d(GC/CG) for inter-platination. Surprisingly, no preferential binding of linker histones to cis-inter-platinated DNA was observed by means of the electromobility-shift assay. The same negative results were obtained with a part of the linker histone molecule suggested to be responsible for DNA-binding--its globular domain. Contrary, the data with another nuclear protein with similar DNA-binding properties as linker histones--HMGB1--showed a strong afinity for interaction with DNA containing interstrand cross-links.
Yaneva
Julia N
JN
Department of Gene Regulations, Institute of Molecular Biology, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria. jyaneva@obzor.bio21.bas.bg
Paneva
Elena G
EG
Zacharieva
Siyka I
SI
Zlatanova
Jordanka S
JS
D001483:Base Sequence; D001665:Binding Sites; D002945:Cisplatin / Q000494:pharmacology*; D003432:Cross-Linking Reagents; D004247:DNA / Q000187:drug effects* / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D009838:Oligodeoxyribonucleotides / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding
D003432:Cross-Linking Reagents; D006657:Histones; D009838:Oligodeoxyribonucleotides; D004247:DNA; D002945:Cisplatin