[Structural organization of DNA complexes with proteins HMGB1 and HMGB1-(A+B)].
The interaction between DNA and the nonhistone proteins HMGB1 and HMGB1-(A+B) has been studied using circular dichroism and scanning force microscopy. The recombinant protein HMGB1-(A+B) has no negatively charged C-terminal domain characteristic for HMGB1. Our earlier suggestion about the structural interaction of tandem HMGB1-domains of the recombinant protein with DNA was confirmed. It was shown that the C-terminal part modulates the interactions of HMGB1-domains with DNA. Without the C-terminal sequence, the HMGB1-(A+B) protein forms DNA-protein complexes with the ordered supramolecular structure.
Polianichko
A M
AM
Leonenko
Z V
ZV
Kramb
D
D
Vieser
G
G
Vorob'ev
V I
VI
Chikhirzhina
E V
EV
D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D004247:DNA / Q000737:chemistry*; D024243:HMGB1 Protein / Q000737:chemistry* / Q000648:ultrastructure; D006801:Humans; D008855:Microscopy, Electron, Scanning; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000648:ultrastructure
D024243:HMGB1 Protein; D011994:Recombinant Proteins; D004247:DNA