6533b874fe1ef96bd12d60f5
RESEARCH PRODUCT
Histone variants from pea (Pisum sativum): Their differential presence in fractions obtained by DNase I digestion of nuclei
M. Isabel RodrigoLuis Francosubject
Gel electrophoresisProteasebiologyPhysiologymedicine.medical_treatmentCell BiologyPlant ScienceGeneral Medicinebiology.organism_classificationPisumChromatinHistoneSativumBiochemistryGeneticsbiology.proteinmedicineDigestionPolyacrylamide gel electrophoresisdescription
The variants of the core histones of Pisum sativum L. cv. Lincoln have been resolved by two dimensional polyacrylamide gel electrophoresis. Acetic acid, 8 M urea, 7.2 mM Triton X-100 was used in the first dimension. The second dimension was run in the presence of either anionic (sodium dodecylsulphate) or cationic (cetyltrimethyl-aminonium bromide) detergents. Four putative variants were found for the H2B histone class, 4 for H3 and 3 for H2A. Peptide mapping with (Staphylococcus aureus V8 protease was used, together with other criteria, to characterize the variants. The pattern of histone variants is not organ specific and, in an attempt to determine whether the diversity of histone variants plays some functional role, the kinetics of release of core histones by extensive DNase I digestion of nuclei was studied. H2A and H2B were released under our conditions of digestion, but the lime course of release of the different H2A variants showed a certain specificity.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1990-04-01 | Physiologia Plantarum |