Dissection of the unusual structural and functional properties of the variant H2A.Bbd nucleosome

Doyen, Cécile Marie; Montel, Fabien; Gautier, Thierry; Menoni, Hervé; Claudet, Cyrille; Delacour-Larose, Marlène; Angelov, Dimitar; Hamiche, Ali; Bednář, Jan; Faivre-Moskalenko, Cendrine; Bouvet, Philippe; Dimitrov, Stéfan

doi:10.1038/sj.emboj.7601310

Cited by 103 publications

(140 citation statements)

References 46 publications

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“…A recent study of the histone variant H2A.Bbd also suggested that the H4 tail might interact with the H2A pocket in an intranucleosomal manner (49). Nucleosome arrays containing H2A.Bbd exhibited an unusually extended conformation in low salt, suggesting that the DNA was partially unwrapped from the edges of the nucleosome, consistent with studies showing H2A.Bbd nucleosomes protect less than 147 bp of DNA from nuclease digestion (4,14). Moreover, it was found that a restored acidic patch on the H2A.Bbd surface works together with the H4 tail to maintain an intact 29 S (normally extended) chromatin conformation in low salt in which the nucleosomes contain DNA that is fully wrapped around the histone octamers (49).…”

Section: Discussionsupporting

confidence: 58%

The H4 Tail Domain Participates in Intra- and Internucleosome Interactions with Protein and DNA during Folding and Oligomerization of Nucleosome Arrays

Kan

Caterino²,

Hayes³

2009

Molecular and Cellular Biology

156

151

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The condensation of nucleosome arrays into higher-order secondary and tertiary chromatin structures likely involves long-range internucleosomal interactions mediated by the core histone tail domains. We have characterized interarray interactions mediated by the H4 tail domain, known to play a predominant role in the formation of such structures. We find that the N-terminal end of the H4 tail mediates interarray contacts with DNA during self-association of oligonucleosome arrays similar to that found previously for the H3 tail domain. However, a site near the histone fold domain of H4 participates in a distinct set of interactions, contacting both DNA and H2A in condensed structures. Moreover, we also find that H4-H2A interactions occur via an intraas well as an internucleosomal fashion, supporting an additional intranucleosomal function for the tail. Interestingly, acetylation of the H4 tail has little effect on interarray interactions by itself but overrides the strong stimulation of interarray interactions induced by linker histones. Our results indicate that the H4 tail facilitates secondary and tertiary chromatin structure formation via a complex array of potentially exclusive interactions that are distinct from those of the H3 tail domain.Eukaryotic DNA is packaged with core histones and other nonhistone chromosomal proteins through multiple levels of increasingly condensed chromatin structures. Arrays of nucleosomes, which form the primary repeating structure of chromatin, fold into secondary chromatin structures such as the 30-nm-diameter chromatin fiber (21, 37, 45). Chromatin fibers and other secondary structures are further condensed into higher-order tertiary chromatin structures such as the 100-to 130-nm-diameter chromonema observed by Belmont and Bruce (7). While models (solenoid, twisted-ribbon, and crossed-linker) have been proposed for the 30-nm-diameter chromatin fiber, to date no definitive model has been broadly accepted (38). Moreover, only very limited structural information is available with regard to tertiary and higher-order chromatin structures (see references 21, 30, and 45 and see below).Although the molecular mechanisms behind the formation of secondary and tertiary chromatin structures remain unclear, work employing model systems has shown that in vitro reconstituted nucleosome arrays containing only DNA and core histone proteins undergo the same initial salt-dependent condensations as native chromatin (17, 21). In solutions containing physiological concentrations of mono-and divalent cations, nucleosome arrays spontaneously fold into structures with the same hydrodynamic shape as the 30-nm-diameter chromatin fiber and reversibly self-associate into larger assemblies with characteristics of native tertiary chromatin structures (21, 45).

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Section: Discussionsupporting

confidence: 58%

The H4 Tail Domain Participates in Intra- and Internucleosome Interactions with Protein and DNA during Folding and Oligomerization of Nucleosome Arrays

Kan

Caterino²,

Hayes³

2009

Molecular and Cellular Biology

156

151

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“…The H2AL2 nucleosome was quite susceptible to nucleases, suggesting that these nucleosomes have different structural properties, as compared to those of the conventional nucleosome (21). A possible human counterpart of H2AL2, H2A.Bbd, which is highly expressed in the testis, was also suggested to form a specific nucleosome structure with reduced stability (22)(23)(24). Furthermore, nucleosomes containing a testis-specific H2B variant, hTSH2B/TH2B, were reportedly unstable, as compared to the conventional nucleosome (25).…”

Section: Discussionmentioning

confidence: 99%

Structural basis of instability of the nucleosome containing a testis-specific histone variant, human H3T

Tachiwana

Kagawa

Osakabe

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

207

236

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A histone H3 variant, H3T, is highly expressed in the testis, suggesting that it may play an important role in the chromatin reorganization required for meiosis and/or spermatogenesis. In the present study, we found that the nucleosome containing human H3T is significantly unstable both in vitro and in vivo, as compared to the conventional nucleosome containing H3.1. The crystal structure of the H3T nucleosome revealed structural differences in the H3T regions on both ends of the central α2 helix, as compared to those of H3.1. The H3T-specific residues (Met71 and Val111) are the source of the structural differences observed between H3T and H3.1. A mutational analysis revealed that these residues are responsible for the reduced stability of the H3T-containing nucleosome. These physical and structural properties of the H3T-containing nucleosome may provide the basis of chromatin reorganization during spermatogenesis.

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“…H2A-Bbd is associated with active chromatin. The structure of its central globular domain allows only 130 bp of DNA to be wrapped around the nucleosome, creating a more relaxed, accessible chromatin structure (Doyen et al, 2006b). H2A.Z is associated with both active and inactive chromatin (Cheung and Lau, 2005).…”

Section: Histone Variantsmentioning

confidence: 99%

Epigenetics in development

Kiefer

2007

Developmental Dynamics

242

144

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It has become increasingly evident in recent years that development is under epigenetic control. Epigenetics is the study of heritable changes in gene function that occur independently of alterations to primary DNA sequence. The best-studied epigenetic modifications are DNA methylation, and changes in chromatin structure by histone modifications, and histone exchange. An exciting, new chapter in the field is the finding that long-distance chromosomal interactions also modify gene expression. Epigenetic modifications are key regulators of important developmental events, including X-inactivation, genomic imprinting, patterning by Hox genes and neuronal development. This primer covers these aspects of epigenetics in brief, and features an interview with two epigenetic scientists. Developmental Dynamics 236: 1144 -1156, 2007.

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Dissection of the unusual structural and functional properties of the variant H2A.Bbd nucleosome

Cited by 103 publications

References 46 publications

The H4 Tail Domain Participates in Intra- and Internucleosome Interactions with Protein and DNA during Folding and Oligomerization of Nucleosome Arrays

The H4 Tail Domain Participates in Intra- and Internucleosome Interactions with Protein and DNA during Folding and Oligomerization of Nucleosome Arrays

Structural basis of instability of the nucleosome containing a testis-specific histone variant, human H3T

Epigenetics in development

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