tailieunhanh - Báo cáo khoa học: Sequence variants of chicken linker histone H1.a

Two allelic isoforms ( and ) of histone were identified within two conservative flocks (R11 and R55) of Rhode Island Red chick-ens. These proteins form three phenotypes: a1, a2 and a1a2. Birds with phenotype a1 were most common (frequency –) while the a1a2 chickens appeared relatively rarely (–). | iFEBS Journal Sequence variants of chicken linker histone Ewa GOrnicka-Michalska1 Jan Patyga1 Andrzej Kowalski1 and Katarzyna Cywa-Benko2 1 Department of Genetics Institute of Biology Akademia Swietokrzyska Kielce Poland 2 Department of AnimalProduction Faculty of Biology and Agriculture Rzeszow University Poland Keywords allelic isoforms chicken genetic polymorphism histone H1 peptide microsequencing Correspondence E. Gornicka-Michalska Department of Genetics Institute of Biology Akademia Swietokrzyska ul. Swietokrzyska 15 25-406 Kielce Poland Fax 48 41 3496292 Tel 48 41 3496333 E-mail egorn@ jpalyga@ Received 22 August 2005 revised 16 January 2006 accepted 19 January 2006 doi Two allelic isoforms and of histone 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 al were most common frequency while the a1a2 chickens appeared relatively rarely . 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 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 polymorphism. As indicated by cleavages with a-chymotrypsin and protease V8 the and 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 allelic isoforms was detected by Edman degradation glutamic acid present at position 117 in histone was replaced by lysine in histone . Furthermore using microsequencing techniques we have found a sequence .