DNA-induced secondary structure of the carboxy-terminal domain of histone H1

doi:10.1074/jbc.M505636200

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Papers In Press, published online ahead of print July 8, 2005
J. Biol. Chem, 10.1074/jbc.M505636200
Submitted on May 23, 2005
Revised on June 27, 2005
Accepted on July 8, 2005

DNA-induced secondary structure of the carboxy-terminal domain of histone H1

Alicia Roque, Ibon Iloro, Imma Ponte, José Luis R. Arrondo, and Pedro Suau

Bioquímica y Biología Molecular, Universidad Autónoma de Barcelona, Bellaterra, Barcelona 08193

Corresponding Author: Pere.Suau{at}uab.es

We have studied the secondary structure of the C-terminal domains of linker histone H1 subtypes H1º (C-H1º) and H1t (C-H1t), free in solution and bound to DNA, by IR spectroscopy. The C-terminal domain has little structure in aqueous solution, but becomes extensively folded upon interaction with DNA. The secondary structure elements present in the bound C-terminal domain include the a-helix, ß-structure, turns and open loops. The structure of the bound domain shows a significant dependence on salt concentration. In low salt (10 mM NaCl), there is a residual amount of random coil, 7% in C-H1º and 12 % in C-H1t. In physiological salt concentrations (140 mM NaCl), the C-termini become fully structured. Under these conditions, C-H1º contained 24 % of a-helix, 25 % of ß-structure, 17 % of open loops and 33 % of turns. The latter component could include a substantial proportion of 310 helix. In spite of their low sequence identity (~30%), the representation of the different structural motifs in C-H1t was similar to that in C-H1º. Examination of the changes in the amide I components in the 20-80ºC temperature interval shows that the secondary structure of the DNA-bound C-H1t is for the most part extremely stable. The H1 C-terminal domain appears to belong to the so-called disordered proteins, undergoing coupled binding and folding.

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