Biochemical properties and localization of the chromosomal protein IP25.
The protein IP25, which has previously been reported to accumulate in the chromatin during erythroid differentiation of Friend-virus-transformed erythroleukemia cells (FL cells), is shown to behave like histone H1 without being structurally related to it. Like H1, IP25 is not released by digestion of FL cells nuclei with DNAse I. After micrococcal digestion IP25 and H1 are differentially distributed in the nucleosome monomers and dimers. This distribution suggests an internucleosomal location for IP25 and H1. Different rates of digestion are observed between nuclei of differentiating and non-differentiating FL cells with both DNAse I and micrococcal nuclease. These differences could be due to the presence of IP25 in the chromatin of differentiating cells.
D002467:Cell Nucleus / Q000032:analysis; D002472:Cell Transformation, Viral; D002843:Chromatin / Q000032:analysis; D002868:Chromosomal Proteins, Non-Histone / Q000032:analysis*; D002999:Clone Cells; D003851:Deoxyribonucleases; D004591:Electrophoresis, Polyacrylamide Gel; D005622:Friend murine leukemia virus; D006657:Histones / Q000032:analysis; D006868:Hydrolysis; D004915:Leukemia, Erythroblastic, Acute / Q000378:metabolism; D009363:Neoplasm Proteins / Q000032:analysis; D013997:Time Factors
D002843:Chromatin; D002868:Chromosomal Proteins, Non-Histone; D006657:Histones; D009363:Neoplasm Proteins; D003851:Deoxyribonucleases