Histone H1 of the garden pea (Pisum sativum L.); composition, developmental changes, allelic polymorphism and inheritance

Kosterin, Oleg E.; Богданова, В. С.; Gorel, F. L.; Розов, С. М.; Trusov, Yuri; Бердников, В. С.

doi:10.1016/0168-9452(94)90255-0

Cited by 25 publications

(42 citation statements)

References 33 publications

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“…A specific role for the histone H1 allelic isoform might be assigned based on the cause and effect relationship between the appearance and/or disappearance of a given allele leading to the characteristic phenotypic effects (Kowalski and Palyga 2012a). The histone H1 allele frequencies were shown to correlate with growth dynamics (Kosterin et al 1994;Bogdanova et al 2007), accumulated temperature of vegetation period (Bogdanova et al 2005), and geographic distribution of plants (Berdnikov et al 1993;Dudnikov 2012), plumage colour in duck (Palyga et al 2000), and the effects of environmental pollution in hare (Lepus europaeus).…”

Section: Discussionmentioning

confidence: 99%

“…Acting as peculiar modifiers of chromatin organization, the histone H1 subtypes may control expression of individual genes that influence many important cellular processes, such as chromosome alignment and segregation (Takata et al 2007), mitotic progression (Green et al 2010), and DNA damage response (Kratzmeier et al 1999;Hashimoto et al 2007). Since histone H1 condensing function is mediated by a specific C-terminal domain amino acid composition (Hansen et al 2006;Lu et al 2009), the alterations in the C-terminal domain amino acid sequence (Kosterin et al 1994;Palyga et al 2000;Gornicka-Michalska et al 2006;Kowalski et al 2011a, b) seem to support functional diversity of these chromatin proteins. A specific role for the histone H1 allelic isoform might be assigned based on the cause and effect relationship between the appearance and/or disappearance of a given allele leading to the characteristic phenotypic effects (Kowalski and Palyga 2012a).…”

Section: Discussionmentioning

confidence: 99%

“…Histone H1 is a family of non-allelic subtypes comprising from six or seven components in birds (Palyga 1991) and plants (Kosterin et al 1994) to eleven members in mammals ). The specific functions of histone H1 subtypes has been inferred from their selective distribution in chromatin (Trollope et al 2010) and differential condensing capabilities (Clausell et al 2009) which may determine formation of active and inactive chromatin regions.…”

Section: Discussionmentioning

confidence: 99%

“…In concert with a variety of non-histone proteins (McBryant et al 2010), the histone H1 regulates transcription, replication, and DNA repair following damage that underlie many cellular processes including cell division, differentiation, and aging (Izzo et al 2008). A functional diversification of histone H1 is linked with its heterogeneous composition reflected by the existence of several non-allelic subtypes in mammals (Parseghian and Hamkalo 2001;Happel and Doenecke 2009), birds (Shannon and Wells 1987;Palyga 1991), and plants (Berdnikov et al 1993, Kosterin et al 1994. Some histone H1 non-allelic subtypes play specialized functions (Kowalski and Palyga 2012a).…”

Section: Introductionmentioning

confidence: 99%

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A shift in erythrocyte histone H1 complement following selection in quail (Coturnix japonica)

et al. 2015

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This work was aimed at comparing distribution of isoforms for polymorphic histone H1 variants H1.b and H1.z and variably abundant histone H1.d subtype between quail (Coturnix japonica) population selected for a high egg yolk cholesterol content and the control birds. The isoforms of histone H1.b (H1.b1, H1.b2) and histone H1.z (H1.z1, H1.z2) differed in their apparent molecular weights judging from their differential migration rates in one-and two-dimensional SDS-polyacrylamide gels. Stained histone H1.d bands and spots in one-dimensional acetic acid-urea and two-dimensional SDS-polyacrylamide gel patterns, respectively, exhibited differential intensities among quail individuals. Histone H1. .f. = 1, P < 0.01) were found to be statistically significant among the control and selected population. In general, a moderate degree of genetic divergence (F ST equal to 0.07 and 0.1 at loci H1.b and H1.z, respectively) was observed among the control and selected quail populations. Selection may directly or indirectly affect the complement of H1 histones because of their presumably differential interactions with DNA and/or DNA-associated proteins resulting in alterations in the chromatin function.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A shift in erythrocyte histone H1 complement following selection in quail (Coturnix japonica)

et al. 2015

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“…In garden pea, seven genes, His1-His7, encoding the various subtypes of histones H1 lie in three regions of the genetic map, with His2-His6 tightly linked Kosterin et al, 1994). Only His1 has been coupled with its DNA sequence (Berdnikov et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Structure of allelic variants of subtype 5 of histone H1 in pea Pisum sativum L.

et al. 2005

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The pea genome contains seven histone H1 genes encoding different subtypes. Previously, the DNA sequence of only one gene, His1, coding for the subtype H1-1, had been identified. We isolated a histone H1 allele from a pea genomic DNA library. Data from the electrophoretic mobility of the pea H1 subtypes and their N-bromosuccinimide cleavage products indicated that the newly isolated gene corresponded to the H1-5 subtype encoded by His5. We confirmed this result by sequencing the gene from three pea lines with H1-5 allelic variants of altered electrophoretic mobility. The allele of the slow H1-5 variant differed from the standard allele by a nucleotide substitution that caused the replacement of the positively charged lysine with asparagine in the DNA-interacting domain of the histone molecule. A temperature-related occurrence had previously been demonstrated for this H1-5 variant in a study on a worldwide collection of pea germplasm. The variant tended to occur at higher frequencies in geographic regions with a cold climate. The fast allelic variant of H1-5 displayed a deletion resulting in the loss of a duplicated pentapeptide in the C-terminal domain. Heredity (2005) 94, 582-588.

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Molecular cloning and expression of mRNAs encoding H1 histone and an H1 histone-like sequences in root tips of pea (Pisum sativum L.)

1995

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Two cDNA clones representing mRNAs, highly expressed in pea root tips, were isolated by mRNA differential display. Ribonuclease protection analyses showed different patterns of expression of these two messages in several pea tissues. Sequence analysis showed that the first clone, PsH1b-40, has 100% homology with a previously isolated H1 histone cDNA, PsH1b. However, it has an additional 30 nt at the 3' end which is absent in PsH1b, suggesting possible multiple polyadenylation sites in the same mRNA. The second clone, PsH1b-41, encodes a deduced 19.5 kDa protein of 185 amino acids with an isoelectric point of 11.5. The putative globular domain of the encoded protein showed 67-71% residue identity with globular domains of 28 kDa pea PsH1b H1 histone and Arabidopsis thaliana H1-1 H1 histone. It has 9 repeating motifs of (T/S)XXK. In the C-terminal domain, there are four lysine-rich repeating motifs of SXK(T/S)PXKKXK which may be involved in chromatin condensation and decondensation. Southern blot analysis of nuclear DNA shows that PsH1-41 belongs to a multigene family.

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Histone H1 of the garden pea (Pisum sativum L.); composition, developmental changes, allelic polymorphism and inheritance

Cited by 25 publications

References 33 publications

A shift in erythrocyte histone H1 complement following selection in quail (Coturnix japonica)

A shift in erythrocyte histone H1 complement following selection in quail (Coturnix japonica)

Structure of allelic variants of subtype 5 of histone H1 in pea Pisum sativum L.

Molecular cloning and expression of mRNAs encoding H1 histone and an H1 histone-like sequences in root tips of pea (Pisum sativum L.)

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