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Conserved molecular structure of the centromeric histone CENH3 in Secale and its phylogenetic relationships

It has been repeatedly demonstrated that the centromere-specific histone H3 (CENH3), a key component of the centromere, shows considerable variability between species within taxa. We determined the molecular structure and phylogenetic relationships of CENH3 in 11 Secale species and subspecies that p...

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Autores principales: Evtushenko, E. V., Elisafenko, E. A., Gatzkaya, S. S., Lipikhina, Y. A., Houben, A., Vershinin, A. V.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5732303/
https://www.ncbi.nlm.nih.gov/pubmed/29247163
http://dx.doi.org/10.1038/s41598-017-17932-8
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author Evtushenko, E. V.
Elisafenko, E. A.
Gatzkaya, S. S.
Lipikhina, Y. A.
Houben, A.
Vershinin, A. V.
author_facet Evtushenko, E. V.
Elisafenko, E. A.
Gatzkaya, S. S.
Lipikhina, Y. A.
Houben, A.
Vershinin, A. V.
author_sort Evtushenko, E. V.
collection PubMed
description It has been repeatedly demonstrated that the centromere-specific histone H3 (CENH3), a key component of the centromere, shows considerable variability between species within taxa. We determined the molecular structure and phylogenetic relationships of CENH3 in 11 Secale species and subspecies that possess distinct pollination systems and are adapted to a wide range of abiotic and biotic stresses. The rye (Secale cereale) genome encodes two paralogous CENH3 genes, which differ in intron-exon structure and are transcribed into two main forms of the protein, αCENH3 and βCENH3. These two forms differ in size and amino acid substitutions. In contrast to the reported differences in CENH3 structure between species within other taxa, the main forms of this protein in Secale species and subspecies have a nearly identical structure except some nonsynonymous substitutions. The CENH3 proteins are strictly controlled by genetic factors responsible for purifying selection. A comparison between Hordeum, Secale and Triticum species demonstrates that the structure of CENH3 in the subtribes Hordeinae and Triticinae evolved at different rates. The assumption that reticulate evolution served as a factor stabilizing the structure and evolutionary rate of CENH3 and that this factor was more powerful within Secale and Triticum than in Hordeum, is discussed.
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spelling pubmed-57323032017-12-21 Conserved molecular structure of the centromeric histone CENH3 in Secale and its phylogenetic relationships Evtushenko, E. V. Elisafenko, E. A. Gatzkaya, S. S. Lipikhina, Y. A. Houben, A. Vershinin, A. V. Sci Rep Article It has been repeatedly demonstrated that the centromere-specific histone H3 (CENH3), a key component of the centromere, shows considerable variability between species within taxa. We determined the molecular structure and phylogenetic relationships of CENH3 in 11 Secale species and subspecies that possess distinct pollination systems and are adapted to a wide range of abiotic and biotic stresses. The rye (Secale cereale) genome encodes two paralogous CENH3 genes, which differ in intron-exon structure and are transcribed into two main forms of the protein, αCENH3 and βCENH3. These two forms differ in size and amino acid substitutions. In contrast to the reported differences in CENH3 structure between species within other taxa, the main forms of this protein in Secale species and subspecies have a nearly identical structure except some nonsynonymous substitutions. The CENH3 proteins are strictly controlled by genetic factors responsible for purifying selection. A comparison between Hordeum, Secale and Triticum species demonstrates that the structure of CENH3 in the subtribes Hordeinae and Triticinae evolved at different rates. The assumption that reticulate evolution served as a factor stabilizing the structure and evolutionary rate of CENH3 and that this factor was more powerful within Secale and Triticum than in Hordeum, is discussed. Nature Publishing Group UK 2017-12-15 /pmc/articles/PMC5732303/ /pubmed/29247163 http://dx.doi.org/10.1038/s41598-017-17932-8 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Evtushenko, E. V.
Elisafenko, E. A.
Gatzkaya, S. S.
Lipikhina, Y. A.
Houben, A.
Vershinin, A. V.
Conserved molecular structure of the centromeric histone CENH3 in Secale and its phylogenetic relationships
title Conserved molecular structure of the centromeric histone CENH3 in Secale and its phylogenetic relationships
title_full Conserved molecular structure of the centromeric histone CENH3 in Secale and its phylogenetic relationships
title_fullStr Conserved molecular structure of the centromeric histone CENH3 in Secale and its phylogenetic relationships
title_full_unstemmed Conserved molecular structure of the centromeric histone CENH3 in Secale and its phylogenetic relationships
title_short Conserved molecular structure of the centromeric histone CENH3 in Secale and its phylogenetic relationships
title_sort conserved molecular structure of the centromeric histone cenh3 in secale and its phylogenetic relationships
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5732303/
https://www.ncbi.nlm.nih.gov/pubmed/29247163
http://dx.doi.org/10.1038/s41598-017-17932-8
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