scholarly journals Phylogeny-Based Systematization of Arabidopsis Proteins with Histone H1 Globular Domain

2017 ◽  
Vol 174 (1) ◽  
pp. 27-34 ◽  
Author(s):  
Maciej Kotliński ◽  
Lukasz Knizewski ◽  
Anna Muszewska ◽  
Kinga Rutowicz ◽  
Maciej Lirski ◽  
...  
Keyword(s):  
Histone H1 ◽  
Globular Domain ◽  
Arabidopsis Proteins

scholarly journals The globular domain of histone H1 is sufficient to direct specific gene repression in early Xenopus embryos

1998 ◽  
Vol 8 (9) ◽  
pp. 533-S2 ◽  
Author(s):  
Danielle Vermaak ◽  
Oliver C. Steinbach ◽  
Stephan Dimitrov ◽  
Ralph A.W. Rupp ◽  
Alan P. Wolffe
Keyword(s):  
Histone H1 ◽  
Gene Repression ◽  
Specific Gene ◽  
Globular Domain ◽  
Xenopus Embryos

Characterization of monomeric DNA-binding protein Histone H1 inLeishmania braziliensis

Parasitology ◽  
2011 ◽  
Vol 138 (9) ◽  
pp. 1093-1101 ◽  
Author(s):  
EMMA CARMELO ◽  
GLORIA GONZÁLEZ ◽  
TERESA CRUZ ◽  
ANTONIO OSUNA ◽  
MARIANO HERNÁNDEZ ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Dna Binding ◽  
Chromatin Condensation ◽  
Histone H1 ◽  
Mass Spectrometry Analysis ◽  
Globular Domain ◽  
Mobility Shift ◽  
Aggregation State ◽  
Genome Database

SUMMARYHistone H1 inLeishmaniapresents relevant differences compared to higher eukaryote counterparts, such as the lack of a DNA-binding central globular domain. Despite that, it is apparently fully functional since its differential expression levels have been related to changes in chromatin condensation and infectivity, among other features. The localization and the aggregation state ofL. braziliensisH1 has been determined by immunolocalization, mass spectrometry, cross-linking and electrophoretic mobility shift assays. Analysis of H1 sequences from theLeishmaniaGenome Database revealed that our protein is included in a very divergent group of histones H1 that is present only inL. braziliensis.An antibody raised against recombinantL. braziliensisH1 recognized specifically that protein by immunoblot inL. braziliensisextracts, but not in otherLeishmaniaspecies, a consequence of the sequence divergences observed amongLeishmaniaspecies. Mass spectrometry analysis andin vitroDNA-binding experiments have also proven thatL. braziliensisH1 is monomeric in solution, but oligomerizes upon binding to DNA. Finally, despite the lack of a globular domain,L. braziliensisH1 is able to form complexes with DNAin vitro, with higher affinity for supercoiled compared to linear DNA.

Homo- and Heteronuclear Two-Dimensional NMR Studies of the Globular Domain of Histone H1: Full Assignment, Tertiary Structure, and Comparison with the Globular Domain of Histone H5

Biochemistry ◽  
1994 ◽  
Vol 33 (37) ◽  
pp. 11079-11086 ◽  
Author(s):  
Corinne Cerf ◽  
Guy Lippens ◽  
V. Ramakrishnan ◽  
Serge Muyldermans ◽  
Alain Segers ◽  
...  
Keyword(s):  
Tertiary Structure ◽  
Histone H1 ◽  
Globular Domain ◽  
Two Dimensional ◽  
Nmr Studies ◽  
Histone H5

The histone H1 family: specific members, specific functions?

2008 ◽  
Vol 389 (4) ◽  
pp. 333-343 ◽  
Author(s):  
Annalisa Izzo ◽  
Kinga Kamieniarz ◽  
Robert Schneider
Keyword(s):  
General Structure ◽  
Distinct Species ◽  
Histone H1 ◽  
Globular Domain ◽  
Compensatory Mechanisms ◽  
Biochemical Analyses ◽  
Related Proteins

AbstractThe linker histone H1 binds to the DNA entering and exiting the nucleosomal core particle and has an important role in establishing and maintaining higher order chromatin structures. H1 forms a complex family of related proteins with distinct species, tissue and developmental specificity. In higher eukaryotes all H1 variants have the same general structure, consisting of a central conserved globular domain and less conserved N-terminal and C-terminal tails. These tails are moderately conserved among species, but differ among variants, suggesting a specific function for each H1 variant. Due to compensatory mechanisms and to the lack of proper tools, it has been very difficult to study the biological role of individual variants in chromatin-mediated processes. Our knowledge about H1 variants is indeed limited, andin vitroandin vivoobservations have often been contradictory. Therefore, H1 variants were considered to be functionally redundant. However, recent knockout studies and biochemical analyses in different organisms have revealed exciting new insights into the specificity and mechanisms of actions of the H1 family members. Here, we collect and compare the available literature about H1 variants and discuss possible specific roles that challenge the concept of H1 being a mere structural component of chromatin and a general repressor of transcription.

scholarly journals Precise elimination of the N-terminal domain of histone H1

1982 ◽  
Vol 203 (3) ◽  
pp. 577-582 ◽  
Author(s):  
L Böhm ◽  
P Sautière ◽  
P D Cary ◽  
C Crane-Robinson
Keyword(s):  
Tertiary Structure ◽  
Submaxillary Gland ◽  
Spectroscopic Characterization ◽  
Histone H1 ◽  
Globular Domain ◽  
Edman Degradation ◽  
Terminal Domain ◽  
C Terminus ◽  
Mouse Submaxillary Gland ◽  
Calf Thymus

The proteinase from mouse submaxillary gland was used to cleave total calf thymus histone H1 between residues 32 and 33. The C-terminal peptide, comprising residues 33 to the C-terminus, was purified and identified by amino acids analysis and Edman degradation. Spectroscopic characterization by n.m.r. for tertiary structure and by c.d. for secondary structure shows the globular domain of the parent histone H1 to be preserved intact in the peptide. It has therefore lost only the N-terminal domain and is a fragment of histone H1 comprising the globular plus C-terminal domains only. Precise elimination of only the N-terminal domain makes the fragment suitable for testing domain function in histone H1.

scholarly journals Binding Dynamics of Disordered Linker Histone H1 with a Nucleosomal Particle

2020 ◽  
Author(s):  
Hao Wu ◽  
Yamini Dalal ◽  
Garegin A. Papoian
Keyword(s):  
Regulatory Protein ◽  
Conformational Dynamics ◽  
Histone H1 ◽  
Linker Histone ◽  
Coarse Grained ◽  
Globular Domain ◽  
Linker Histone H1 ◽  
Eukaryotic Chromatin ◽  
Cancer Phenotype ◽  
Terminal Domains

AbstractLinker histone H1 is an essential regulatory protein for many critical biological processes, such as eukaryotic chromatin packaging and gene expression. Mis-regulation of H1s is commonly observed in tumor cells, where the balance between different H1 subtypes has been shown to alter the cancer phenotype. Consisting of a rigid globular domain and two highly charged terminal domains, H1 can bind to multiple sites on a nucleosomal particle to alter chromatin hierarchical condensation levels. In particular, the disordered H1 amino- and carboxyl-terminal domains (NTD/CTD) are believed to enhance this binding affinity, but their detailed dynamics and functions remain unclear. In this work, we used a coarse-grained computational model AWSEM-DNA to simulate the H1.0b-nucleosome complex, namely chromatosome. Our results demonstrate that H1 disordered domains restrict the dynamics of both globular H1 and linker DNA arms, resulting in a more compact and rigid chromatosome particle. Furthermore, we identified regions of H1 disordered domains that are tightly tethered to DNA near the entry-exit site. Overall, our study elucidates at near atomic resolution the way the disordered linker histone H1 modulates nucleosome’s structural preferences and conformational dynamics.

scholarly journals Histone H1 Is Required for Proper Regulation of Pyruvate Decarboxylase Gene Expression in Neurosporacrassa

2003 ◽  
Vol 2 (2) ◽  
pp. 341-350 ◽  
Author(s):  
H. Diego Folco ◽  
Michael Freitag ◽  
Ana Ramón ◽  
Esteban D. Temporini ◽  
María E. Alvarez ◽  
...  
Keyword(s):  
Chromosome Segregation ◽  
Fluorescent Protein ◽  
Carbon Sources ◽  
Pyruvate Decarboxylase ◽  
Chimeric Protein ◽  
Gene Promoter ◽  
Histone H1 ◽  
Globular Domain ◽  
Mutagen Sensitivity ◽  
Green Fluorescent

ABSTRACT We show that Neurospora crassa has a single histone H1 gene, hH1, which encodes a typical linker histone with highly basic N- and C-terminal tails and a central globular domain. A green fluorescent protein-tagged histone H1 chimeric protein was localized exclusively to nuclei. Mutation of hH1 by repeat-induced point mutation (RIP) did not result in detectable defects in morphology, DNA methylation, mutagen sensitivity, DNA repair, fertility, RIP, chromosome pairing, or chromosome segregation. Nevertheless, hH1 mutants had mycelial elongation rates that were lower than normal on all tested carbon sources. This slow linear growth phenotype, however, was less evident on medium containing ethanol. The pyruvate decarboxylase gene, cfp, was abnormally derepressed in hH1 mutants on ethanol-containing medium. This derepression was also found when an ectopically integrated fusion of the cfp gene promoter to the reporter gene hph was analyzed. Thus, Neurospora histone H1 is required for the proper regulation of cfp, a gene with a key role in the respiratory-fermentative pathway.

scholarly journals The primary structure of a minor isoform (H1.2) of histone H1 from the nematode Caenorhabditis elegans

1990 ◽  
Vol 265 (3) ◽  
pp. 739-746 ◽  
Author(s):  
J R Vanfleteren ◽  
S M Van Bun ◽  
I De Baere ◽  
J J Van Beeumen
Keyword(s):  
Amino Acid ◽  
Caenorhabditis Elegans ◽  
Secondary Structure ◽  
Alpha Helix ◽  
Histone H1 ◽  
Globular Domain ◽  
Nematode Caenorhabditis Elegans ◽  
Terminal Domain ◽  
Helix Formation ◽  
A Minor

The complete amino acid sequence of a minor isoform (H1.2) of histone H1 from the nematode Caenorhabditis elegans was determined. The amino acid chain consists of 190 residues and has a blocked N-terminus. Histone subtype H1.2 is 17 residues shorter than the major isoform H1.1, mainly as the result of deletions of short peptide fragments. Considerable divergence from isoform H1.1 has occurred in the N-terminal domain and the very C-terminus of the molecule, but the central globular domain and most of the C-terminal domain, including two potential phosphorylation sites, have been well conserved. Secondary-structure predictions for both H1 isoforms reveal a high potential for helix formation in the N-terminal region 1-33 of isoform H1.1 whereas the corresponding region in isoform H1.2 has low probability of being found in alpha-helix. No major differences in secondary structure are predicted for other parts of both H1 subtypes. The aberrant conformation of isoform H1.2 may be indicative of a significantly different function.

scholarly journals Structurally divergent histone H1 variants in chromosomes containing highly condensed interphase chromatin.

1994 ◽  
Vol 127 (6) ◽  
pp. 1789-1798 ◽  
Author(s):  
E Schulze ◽  
S Nagel ◽  
K Gavenis ◽  
U Grossbach
Keyword(s):  
Histone H1 ◽  
Globular Domain ◽  
Amino Acid Residues ◽  
Sequence Repeat ◽  
Interphase Chromatin ◽  
Volvox Carteri ◽  
Condensed Chromosome ◽  
Core Histones ◽  
Sea Urchin Sperm ◽  
I Gene

Condensed and late-replicating interphase chromatin in the Dipertan insect Chironomus contains a divergent type of histone H1 with an inserted KAP-KAP repeat that is conserved in single H1 variants of Caenorhabditis elegans and Volvox carteri. H1 peptides comprising the insertion interact specifically with DNA. The Chironomid Glyptotendipes exhibits a corresponding correlation between the presence of condensed chromosome sections and the appearance of a divergent H1 subtype. The centromere regions and other sections of Glyptotendipes barbipes chromosomes are inaccessible to immunodecoration by anti-H2B and anti-H1 antibodies one of which is known to recognize nine different epitopes in all domains of the H1 molecule. Microelectrophoresis of the histones from manually isolated unfixed centromeres revealed the presence of H1 and core histones. H1 genes of G. barpipes were sequenced and found to belong to two groups. H1 II and H1 III are rather similar but differ remarkably from H1 I. About 30% of the deduced amino acid residues were found to be unique to H1 I. Most conspicuous is the insertion, SPAKSPGR, in H1 I that is lacking in H1 II and H1 III and at its position gives rise to the sequence repeat SPAKSPAKSPGR. The homologous H1 I gene in Glyptotendipes salinus encodes the very similar repeat TPAKSPAKSPGR. Both sequences are structurally related to the KAPKAP repeat in H1 I-1 specific for condensed chromosome sites in Chironomus and to the SPKKSPKK repeat in sea urchin sperm H1, lie at almost the same distance from the central globular domain, and could interact with linker DNA in packaging condensed chromatin.

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