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Sequence variants of chicken linker histone H1.a
Author(s) -
GórnickaMichalska Ewa,
Pałyga Jan,
Kowalski Andrzej,
CywaBenko Katarzyna
Publication year - 2006
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2006.05147.x
Subject(s) - linker , sequence (biology) , histone h1 , genetics , computational biology , histone , computer science , biology , dna , programming language
Two allelic isoforms (H1.a1 and H1.a2) of histone H1.a were identified within two conservative flocks (R11 and R55) of Rhode Island Red chickens. These proteins form three phenotypes: a1, a2 and a1a2. Birds with phenotype a1 were most common (frequency 0.825–0.980) while the a1a2 chickens appeared relatively rarely (0.017–0.175). The third phenotype a2, not detected in the tested populations, has only been revealed in progeny of the purpose‐mated a1a2 birds. The polymorphism of histone H1.a was observed in all examined chicken tissues, so that the H1 preparations isolated from the lung, spleen, kidney and testis from the same individual exhibited identical phenotypes (a1, a2, or a1a2). This finding, together with inheritance data, supports the genetic nature of the H1.a polymorphism. As indicated by cleavages with α‐chymotrypsin and protease V8, the H1.a1 and H1.a2 are two highly related proteins which differ within N‐terminal part of their C‐terminal tails. Only a single nonconservative amino acid substitution between both H1.a allelic isoforms was detected by Edman degradation: glutamic acid present at position 117 in histone H1.a1 was replaced by lysine in histone H1.a2. Furthermore, using microsequencing techniques we have found a sequence homology between the N‐ and C‐terminal parts of an unknown minor protein H1.y, present in the phenotype a2, and similar regions of histone H1.b.