{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Swygert SG"],"funding":["HHS | NIH | National Institute of General Medical Sciences","HHS | NIH | National Cancer Institute","NIAID NIH HHS","NCI NIH HHS","HHS | NIH | National Institute of Allergy and Infectious Diseases","NIGMS NIH HHS"],"pagination":["12447-12452"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6298083"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["115(49)"],"pubmed_abstract":["Heterochromatin is a silenced chromatin region essential for maintaining genomic stability and driving developmental processes. The complicated structure and dynamics of heterochromatin have rendered it difficult to characterize. In budding yeast, heterochromatin assembly requires the SIR proteins-Sir3, believed to be the primary structural component of SIR heterochromatin, and the Sir2-4 complex, responsible for the targeted recruitment of SIR proteins and the deacetylation of lysine 16 of histone H4. Previously, we found that Sir3 binds but does not compact nucleosomal arrays. Here we reconstitute chromatin fibers with the complete complement of SIR proteins and use sedimentation velocity, molecular modeling, and atomic force microscopy to characterize the stoichiometry and conformation "],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["SIR proteins create compact heterochromatin fibers."],"pmcid":["PMC6298083"],"funding_grant_id":["R01 GM054096","GM54096","U54 CA143862","R01AI117839","R01 AI117839","R35 GM122519"],"pubmed_authors":["Senapati S","Wolfe SA","Swygert SG","Lindsay S","Bolukbasi MF","Peterson CL"],"additional_accession":[]},"is_claimable":false,"name":"SIR proteins create compact heterochromatin fibers.","description":"Heterochromatin is a silenced chromatin region essential for maintaining genomic stability and driving developmental processes. The complicated structure and dynamics of heterochromatin have rendered it difficult to characterize. In budding yeast, heterochromatin assembly requires the SIR proteins-Sir3, believed to be the primary structural component of SIR heterochromatin, and the Sir2-4 complex, responsible for the targeted recruitment of SIR proteins and the deacetylation of lysine 16 of histone H4. Previously, we found that Sir3 binds but does not compact nucleosomal arrays. Here we reconstitute chromatin fibers with the complete complement of SIR proteins and use sedimentation velocity, molecular modeling, and atomic force microscopy to characterize the stoichiometry and conformation ","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Dec","modification":"2025-04-19T16:32:27.613Z","creation":"2019-07-01T13:43:30Z"},"accession":"S-EPMC6298083","cross_references":{"pubmed":["30455303"],"doi":["10.1073/pnas.1810647115"]}}