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Mesoscale simulations of two nucleosome-repeat length oligonucleosomes.

ABSTRACT: The compaction of chromatin, accessed through coarse-grained modeling and simulation, reveals different folding patterns as a function of the nucleosome repeat length (NRL), the presence of the linker histone, and the ionic strength. Our results indicate that the linker histone has negligible influence on short NRL fibers, whereas for longer NRL fibers it works like, and in tandem with, concentrated positive counterions to condense the chromatin fiber. Longer NRL fibers also exhibit structural heterogeneity, with solenoid-like conformations viable in addition to irregular zigzags. These features of chromatin and associated internucleosomal patterns presented here help interpret structural dependencies of the chromatin fiber on internal and external factors. In particular, we suggest that longer-NRL are more advantageous for packing and achieving various levels of fiber compaction throughout the cell cycle.

SUBMITTER: Schlick T

PROVIDER: S-EPMC3182521 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature

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Mesoscale simulations of two nucleosome-repeat length oligonucleosomes.

Schlick Tamar T Perisić Ognjen O

Physical chemistry chemical physics : PCCP 20091020 45

The compaction of chromatin, accessed through coarse-grained modeling and simulation, reveals different folding patterns as a function of the nucleosome repeat length (NRL), the presence of the linker histone, and the ionic strength. Our results indicate that the linker histone has negligible influence on short NRL fibers, whereas for longer NRL fibers it works like, and in tandem with, concentrated positive counterions to condense the chromatin fiber. Longer NRL fibers also exhibit structural h ...[more]

PMID: 20145817

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Project description:Interactions of chromatin with bivalent immunoglobin nucleosome-binding antibodies and their monovalent (papain-derived) antigen-binding fragment analogs are useful probes for examining chromatin conformational states. To help interpret antibody-chromatin interactions and explore how antibodies might compete for interactions with chromatin components, we incorporate coarse-grained PL2-6 antibody modeling into our mesoscale chromatin model. We analyze interactions and fiber structures for the antibody-chromatin complexes in open and condensed chromatin, with and without H1 linker histone (LH). Despite minimal and transient interactions at physiological salt, we capture significant differences in antibody-chromatin complex configurations in open fibers, with more intense interactions between the bivalent antibody and chromatin compared to monovalent antigen-binding fragments. For these open chromatin fiber morphologies, antibody binding to histone tails is increased and compaction is greater for bivalent compared to monovalent and antibody-free systems. Differences between monovalent and bivalent binding result from antibody competition with internal chromatin fiber components (nucleosome core and linker DNA) for histone tail (H3, H4, H2A, H2B) interactions. This antibody competition for tail contacts reduces tail-core and tail-linker interactions and increases tail-antibody interactions. Such internal structural changes in open fibers resemble mechanisms of LH condensation, driven by charge screening and entropy changes. For condensed fibers at physiological salt, the three systems are much more similar overall, but some subtle tail interaction differences can be noted. Adding LH results in less-dramatic changes for all systems, except that the bivalent complex at physiological salt shows cooperative effects between LH and the antibodies in condensing chromatin fibers. Such dynamic interactions that depend on the internal structure and complex-stabilizing interactions within the chromatin fiber have implications for gene regulation and other chromatin complexes such as with LH, remodeling proteins, and small molecular chaperones that bind and modulate chromatin structure.

Dataset Information

Mesoscale simulations of two nucleosome-repeat length oligonucleosomes.

Publications

Mesoscale simulations of two nucleosome-repeat length oligonucleosomes.

Similar Datasets

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