Genetic polymorphism of erythrocyte histone H1 in Japanese quail

Abstract

Histone H1 from erythrocytes of Japanese quail was resolved in a sodium dodecyl sulfate (SDS)-polyacrylamide gel into five fractions differing in apparent molecular weights. A polymorphism of histone H1.1, H1.2, and H1.3 bands was detected among quail individuals. While some birds possessed either a high (phenotype .3+) or a low (phenotype .3+/.3-) level of H1.3, at least half of the quail population lacked this H1 band (phenotype .3-). Appropriate genetic crosses demonstrated that H1.3 behaved as though it was coded by a gene with two codominant alleles at an autosomal locus. Using two-dimensional polyacrylamide gel electrophoresis (acid-urea followed by SDS gels), it was found that birds .3+ contained polypeptides H1.b1 and H1.b'1; birds .3-, polypeptides H1.b2 and H1.b'2 with lower apparent molecular weights; and birds .3+/.3-, both types of polypeptides in equal proportions. The H1.b2 + H1.b'2 complement was not discernible in SDS gels, for it migrated together with H1.c' within band H1.4. It was found that a small number of birds lacking the H1.2 band in SDS gels failed to express histone H1.a. Since birds with phenotype .2- with a defective allele of the gene H1.a were simultaneously lacking the H1.3 band, it seems that the imperfect allele of the H1.a gene might be closely linked to the alleles producing H1.b2 + H1.b'2.

Isolation and preliminary characterization of histone H1.b allelic variants from quail erythrocytes

“…First we identified which phenotypes of the polymorphic histone H1.b were present in these quail strains. As in the previous study (Palyga 1991a) conducted with Pharaoh quail, we found, using one-dimensional SDS-PAGE, that in some birds a histone H1.3 band ( Fig. 2A and B) was either more dense than a faster migrating band H1.4 (phenotype 3 + ), less heavily stained in others (phenotype 3 + 3 -), or completely absent (phenotype 3 -) (Fig.…”

“…The H1 protein complement was separated by electrophoresis either in a 12.5% polyacrylamide gel containing sodium dodecyl sulfate (SDS) or in a 15% polyacrylamide gel containing acetic acid and urea (Palyga 1991a;Neelin et al 1995). The banding pattern and nomenclature of histone H1 variants in one-dimensonal SDS gel is presented in Fig.…”

“…In addition to nonallelic heterogeneity in this family, several linker histone subtypes from various avian species were found to be polymorphic (Greenaway and Murray 1971;Gorel et al 1982;Palyga 1990Palyga , 1991aPalyga , 1991bPalyga et al 1993;Neelin et al 1995); thus variants were detected at three loci during electrophoretic screening of erythrocyte H1 histones of a quail population (Palyga 1991a).…”

“…In this work an attempt was made to isolate allelic variants of the polymorphic histone subtype H1.b from quail erythrocytes (Palyga 1991a) for subsequent comparisons by polyacrylamide gel electrophoresis (PAGE) after cutting with chemical agents or proteolytic enzymes. First, we sought to obtain preparations of purified allelic H1.b proteins from birds with a particular phenotype for this protein by using chromatographic separation of total H1 histones on cation-exchange resin Amberlite CG-50, after having removed histone H5 by gel-permeation chromatography on Bio-Gel P-150.…”

High-Resolution Two-Dimensional Polyacrylamide Gel Electrophoresis: A Tool for Identification of Polymorphic and Modified Linker Histone Components

“…7). As highly basic proteins do not differ enough in both net charge and molecular mass to be fully separated by one-dimensional AU-PAGE (Pałyga, 1991b) or SDS-PAGE , the effective resolution is often achieved by using 2D-PAGE in which non-allelic members of linker histone differing in both parameters are visible.…”