Abstract
Two isoforms of the erythrocyte histone H1.a were identified in two conservative flocks of Rhode Island Red chickens and six conservative flocks of ducks. The H1.a1 and H1.a2 isoforms formed three phenotypes (a1, a2 and a1a2) and were electrophoretically similar in the two species. The frequency of phenotype and histone H1.a allele occurrence varied within the genetic groups of birds, but the relatively rare allele a 2 was only detected in chicken and duck strains with colored feathers. Using mass spectrometry, we established that the difference between the measured masses of the duck H1.a isoforms was 156 Da. Since this value corresponds to the mass of the arginine residue alone or to the combined mass of the valine and glycine residues, we believe that the polymorphism of duck histone H1.a might have originated from sequence variation. A mass difference of 1 Da observed between chicken H1.a isoforms corresponded well to the previously detected Glu/Lys substitution (0.9414 Da) at position 117.
Highlights
The vertebrate histone H1 family consists of a number of variants encoded by distinct genes [1]
Six H1 subtypes were detected in the polyacrylamide gel patterns of total histone H1 preparations from chicken and duck erythrocytes [8, 9]
Two allelic isoforms of the erythrocyte histone H1.a were found [8, 9] in chicken and duck populations
Summary
The vertebrate histone H1 family consists of a number of variants encoded by distinct genes [1]. We performed a partial sequence analysis and molecular mass determination of duck histone H1.a isoforms to identify possible alterations to their C-terminal domain sequences.
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