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Involvement of the histidine residues in the pH-induced conformational change of histone H5

1985; Elsevier BV; Volume: 241; Issue: 2 Linguagem: Inglês

10.1016/0003-9861(85)90596-x

1096-0384

Mitsuhiro Shimidzu, Heisaburo Shindo, Ushiho Matsumoto, Kazuei Mita, Mitsuo Zama,

Enzyme Structure and Function

Comparative studies on the conformational stability of histones H1 and H5 have been carried out by monitoring the pH-induced conformational transitions of the proteins by CD and 1H NMR spectroscopies. The transition point of H1 agrees with the pKa of the carboxyl groups of the acidic residues. In contrast, the transition of H5 is associated with the ionization of the histidine residues which exist exclusively in H5, as well as the deionization of the acidic residues. These observations, combined with the result of the deuterium exchange rates of the histidine C-2 protons, led us to conclude that His-25 and His-62, which are buried in the globular domain, play an important role in the conformational stability of histone H5.