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A K52Q substitution in the globular domain of histone H1t modulates its nucleosome binding properties
Author(s) -
Ramesh Sneha,
Bharath M.M. Srinivas,
Chandra Nagasuma R.,
Rao Manchanahalli R. Satyanarayana
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.09.061
Subject(s) - nucleosome , chromatosome , histone octamer , chemistry , linker dna , histone , histone h1 , histone h2a , biochemistry , biophysics , dna , microbiology and biotechnology , biology
A comparison of the globular domain sequences of the somatic H1d and testis‐specific H1t revealed a single substitution of lysine 52 in H1d to glutamine 54 in H1t, which is one of the three crucial residues within the second DNA binding site. The globular domains of both histones were modeled using the crystal structure of chicken GH5 as a template and was also docked onto the nucleosome structure. The glutamine residue in histone H1t forms a hydrogen bond with main chain carbonyl of methionine‐52 (in H1t) and is spatially oriented away from the nucleosome dyad axis. A consequence of this change was a lower affinity of recombinant histone H1t towards Four‐way junction DNA and reconstituted 5S mononucleosomes. When Gln‐54 in Histone H1t was mutated to lysine, its binding affinity towards DNA substrates was comparable to that of histone H1d. The differential binding of histones H1d and H1t towards reconstituted mononucleosomes was also reflected in the chromatosome‐stop assay.