1: Biochemistry  1985 Mar 12;24(6):1291-7 

Increased stability of the higher order structure of chicken erythrocyte
chromatin: nanosecond anisotropy studies of intercalated ethidium.

Ashikawa I, Kinosita K Jr, Ikegami A, Nishimura Y, Tsuboi M.

Internal motion of the DNA in chicken erythrocyte chromatin fibers was studied
by measurement of the fluorescence anisotropy decay of ethidium intercalated in
the linker region. A comparison of the decay curves of the dye in chicken
erythrocyte chromatin with those of calf thymus chromatin [Ashikawa, I.,
Kinosita, K., Jr., Ikegami, A., Nishimura, Y., Tsuboi, M., Watanabe, K., Iso,
K., & Nakano, T. (1983) Biochemistry 22, 6018-6026] revealed greater suppression
of nucleosome movement in chicken erythrocyte chromatin. Furthermore, the
transition of this chromatin to the compact (solenoidal) structure occurred at
lower solvent concentrations of Na+ or Mg2+ than those for calf thymus
chromatin. These results demonstrated increased stability of the higher order
structure (the solenoid) of chicken erythrocyte chromatin, which may be related
to the reduction of nuclear activity in the chicken erythrocyte cell. In
addition to intact chicken erythrocyte chromatin, we studied the structural
transitions of H1-depleted and H1,H5-depleted chromatins. The result indicated
that histone H5 of this chromatin stabilizes the higher order structure in the
presence of magnesium (or divalent) cation and did not induce the transition in
the solution containing only sodium cation.

PMID: 3986177 [PubMed - indexed for MEDLINE]