Linker histone subtype composition and affinity for chromatin in situ in nucleated mature erythrocytes
2002 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, Vol. 277, no 47, 44688-44694 p.Article in journal (Refereed) Published
The replacement linker histones H10 and H5 are present in frog and chicken erythrocytes, respectively, and their accumulation coincides with cessation of proliferation and compaction of chromatin. These cells have been analyzed for the affinity of linker histones for chromatin with cytochemical and biochemical methods. Our results show a stronger association between linker histones and chromatin in chicken erythrocyte nuclei than in frog erythrocyte nuclei. Analyses of linker histones from chicken erythrocytes using capillary electrophoresis showed H5 to be the subtype strongest associated with chromatin. The corresponding analyses of frog erythrocyte linker histones using reverse-phase high performance liquid chromatography showed that H10 dissociated from chromatin at somewhat higher ionic strength than the three additional subtypes present in frog blood but at lower ionic strength than chicken H5. Which of the two H10 variants in frog is expressed in erythrocytes has thus far been unknown. Amino acid sequencing showed that H10-2 is the only H10 subtype present in frog erythrocytes and that it is 100% acetylated at its N termini. In conclusion, our results show differences between frog and chicken linker histone affinity for chromatin probably caused by the specific subtype composition present in each cell type. Our data also indicate a lack of correlation between linker histone affinity and chromatin condensation.
Place, publisher, year, edition, pages
2002. Vol. 277, no 47, 44688-44694 p.
National CategoryMedical and Health Sciences
IdentifiersURN: urn:nbn:se:liu:diva-14128DOI: 10.1074/jbc.M203533200OAI: oai:DiVA.org:liu-14128DiVA: diva2:22682