All four core histone N-termini contain sequences required for the repression of basal transcription in yeast.

Lenfant, F.; Mann, Randall K.; Thomsen, Bo; Ling, Xuefeng B.; Grunstein, Michael

doi:10.1002/j.1460-2075.1996.tb00771.x

Cited by 86 publications

(73 citation statements)

References 68 publications

(140 reference statements)

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“…This is strongly supported by the observation that a deletion of the histone H2B cross-linking domain changes the minichromosome topology in vivo, suggesting that this domain is required for the proper folding of DNA in the nucleosome (63). Deletion or substitution of a single amino acid in the cross-linking domain of histone H4 alters chromatin structure in vivo (63)(64)(65)(66), decreases the ability of yeast to mate, increases the duration of S phase (67)(68)(69)(70), and affects telomeric repression (71,72) as well as expression of a large number of yeast genes (64,65,(73)(74)(75). It should be mentioned also that the cross-linking domain of histone H4 contains sites for post-translational acetylation and phosphorylation (76) that may also be involved in the regulation of the interaction of this domain with DNA at different levels of chromatin activity and condensation rendering nucleosomes competent for transcription and/or replication.…”

Section: The Change In Histone H2b/h4-dna Contacts Induced By Low Ionmentioning

confidence: 71%

Nucleosome Structural Transition during Chromatin Unfolding Is Caused by Conformational Changes in Nucleosomal DNA

Gavin¹,

Usachenko²,

Bavykin

1998

Journal of Biological Chemistry

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We have recently reported that certain core histone-DNA contacts are altered in nucleosomes during chromatin unfolding (Usachenko, S. I., Gavin I. M., and Bavykin, S. G. (1996) J. Biol. Chem. 271, 3831-3836). In this work, we demonstrate that these alterations are caused by a conformational change in the nucleosomal DNA. Using zero-length protein-DNA cross-linking, we have mapped histone-DNA contacts in isolated core particles at ionic conditions affecting DNA stiffness, which may change the nucleosomal DNA conformation. We found that the alterations in histone-DNA contacts induced by an increase in DNA stiffness in isolated core particles are identical to those observed in nucleosomes during chromatin unfolding. The change in the pattern of micrococcal nuclease digestion of linker histone-depleted chromatin at ionic conditions affecting chromatin compaction also suggests that the stretching of the linker DNA may alter the nucleosomal DNA conformation, resulting in a structural transition in the nucleosome which may play a role in rendering the nucleosome competent for transcription and/or replication.

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Section: The Change In Histone H2b/h4-dna Contacts Induced By Low Ionmentioning

confidence: 71%

Nucleosome Structural Transition during Chromatin Unfolding Is Caused by Conformational Changes in Nucleosomal DNA

Gavin¹,

Usachenko²,

Bavykin

1998

Journal of Biological Chemistry

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“…The presence of histones in chromatin affects chromatin condensation state, binding of transcription factors and promotes basal repression of transcription (Boeger et al, 2003;Boeger et al, 2004;Lenfant et al, 1996;Recht et al, 1996). Thus, lamin-histone H2A interactions could regulate gene expression by interfering with the ability of the nucleosomes to detach from DNA, and thus interfere with chromatin decondensation.…”

Section: Discussionmentioning

confidence: 99%

Specific and conserved sequences inD. melanogasterandC. eleganslamins and histone H2A mediate the attachment of lamins to chromosomes

Mattout

Goldberg

Tzur

et al. 2007

Journal of Cell Science

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The intimate association between nuclear lamins and chromatin is thought to regulate higher order chromatin organization. Previous studies have mapped a region between the rod domain and the Ig fold in the tail domain of Drosophila melanogaster lamin Dm0, which binds chromatin in vitro via the histone H2A/H2B dimer. This region contains an evolutionarily conserved nuclear localization signal (NLS) KRKR, and a sequence composed of the amino acids TRAT. Here we show that binding of lamin Dm0 to chromatin requires both NLS and TRAT sequences. Substituting either of the threonine residues in the TRAT sequence with negatively charged residues decreases the binding of lamin Dm0 to chromatin, indicating that this binding could be regulated by phosphorylation. Both lamin Dm0 and C. elegans Ce-lamin bind directly to histone H2A in vitro and this binding requires the NLS. The amino and carboxyl tail domains of histone H2A are each essential, but not sufficient, for binding to lamin Dm0; only a polypeptide containing both histone H2A tail domains binds efficiently to lamin Dm0. Taken together, these results suggest that specific residues in lamin Dm0 and histone H2A mediate the attachment of the nuclear lamina to chromosomes in vivo, which could have implications on the understanding of laminopathic diseases.

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“…Deletion of amino acids 30 to 37 in the H2B N-terminal domain, which is lethal in some strain backgrounds (19), results in a loss of repression of basal transcription from the GAL1 promoter (11). Mutations in the histone H2B N-terminal domain have shown genetic interactions with the SPT4, SPT5, and SPT6 genes (18) and the SNF5 gene (19), which encodes a component of the SWI/SNF nucleosome-remodeling complex (12).…”

mentioning

confidence: 99%

Deciphering the Roles of the Histone H2B N-Terminal Domain in Genome-Wide Transcription

Parra

Kerr

Fahy

et al. 2006

Molecular and Cellular Biology

123

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Histone N-terminal domains are frequent targets of posttranslational modifications. Multiple acetylated lysine residues have been identified in the N-terminal domain of H2B (K6, K11, K16, K17, K21, and K22), but little is known about how these modifications regulate transcription. We systematically mutated the N-terminal domain of histone H2B, both at known sites of lysine acetylation and elsewhere, and characterized the resulting changes in genome-wide expression in each mutant strain. Our results indicate that known sites of lysine acetylation in this domain are required for gene-specific transcriptional activation. However, the entire H2B N-terminal domain is principally required for the transcriptional repression of a large subset of the yeast genome. We find that the histone H2B repression (HBR) domain, comprised of residues 30 to 37, is necessary and sufficient for this repression. Many of the genes repressed by the HBR domain are located adjacent to telomeres or function in vitamin and carbohydrate metabolism. Deletion of the HBR domain also confers an increased sensitivity to DNA damage by UV irradiation. We mapped the critical residues in the HBR domain required for its repression function. Finally, comparisons of these data with previous studies reveal that a surprising number of genes are coregulated by the N-terminal domains of histone H2B, H3, and H4.In eukaryotic cells, DNA is packaged with histones and other proteins into chromatin (5). The principal packaging unit is the nucleosome, which consists of approximately 147 bp of DNA wrapped around a protein core of one histone H3-H4 tetramer and two histone H2A-H2B dimers (21). Because of their close association with DNA in the nucleosome, histones play integral roles in DNA-templated processes, such as DNA transcription, replication, and repair. Each of the four histone proteins is covalently modified at multiple residues, principally in their flexible N-terminal domains (9, 15). Histone modifications, such as lysine acetylation, lysine methylation, and serine phosphorylation, profoundly affect transcription initiation by regulating the association of transcriptional regulatory proteins with DNA (2, 10, 30).While modifications in the N-terminal domains of histone H3 and H4 have been extensively studied, relatively little is known about how N-terminal modifications in histone H2A and H2B regulate transcription. In Saccharomyces cerevisiae, histone H2B is acetylated at six lysine residues in its N-terminal domain (K6, K11, K16, K17, K21, and K22), most likely by the Gcn5 histone acetyltransferase (24, 28). H2B-K16 has been shown to be hypoacetylated in regions of subtelomeric heterochromatin due to the actions of the Hda1 histone deacetylase (23). It is unclear, however, whether there is a functional requirement for histone H2B hypoacetylation in subtelomeric heterochromatin. The histone H2B N-terminal domain does not appear to regulate telomeric silencing (29, 32).Deletion of amino acids 30 to 37 in the H2B N-terminal domain, which is lethal in some s...

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All four core histone N-termini contain sequences required for the repression of basal transcription in yeast.

Cited by 86 publications

References 68 publications

Nucleosome Structural Transition during Chromatin Unfolding Is Caused by Conformational Changes in Nucleosomal DNA

Nucleosome Structural Transition during Chromatin Unfolding Is Caused by Conformational Changes in Nucleosomal DNA

Specific and conserved sequences inD. melanogasterandC. eleganslamins and histone H2A mediate the attachment of lamins to chromosomes

Deciphering the Roles of the Histone H2B N-Terminal Domain in Genome-Wide Transcription

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