{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["McGowan S"],"funding":["NIGMS NIH HHS"],"pagination":["3144-55"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC1500978"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["25(13)"],"pubmed_abstract":["Most serpins are associated with protease inhibition, and their ability to form loop-sheet polymers is linked to conformational disease and the human serpinopathies. Here we describe the structural and functional dissection of how a unique serpin, the non-histone architectural protein, MENT (Myeloid and Erythroid Nuclear Termination stage-specific protein), participates in DNA and chromatin condensation. Our data suggest that MENT contains at least two distinct DNA-binding sites, consistent with its simultaneous binding to the two closely juxtaposed linker DNA segments on a nucleosome. Remarkably, our studies suggest that the reactive centre loop, a region of the MENT molecule essential for chromatin bridging in vivo and in vitro, is able to mediate formation of a loop-sheet oligomer. Thes"],"journal":["The EMBO journal"],"pubmed_title":["X-ray crystal structure of MENT: evidence for functional loop-sheet polymers in chromatin condensation."],"pmcid":["PMC1500978"],"funding_grant_id":["R01 GM059118","GM-59118"],"pubmed_authors":["Kan WT","Bulynko YA","Rossjohn J","Ong PC","Smith AI","McGowan S","Irving JA","Bottomley SP","Whisstock JC","Buckle AM","Henderson KN","Bashtannyk-Puhalovich TA","Pike RN","Grigoryev SA","Popova EY"],"additional_accession":[]},"is_claimable":false,"name":"X-ray crystal structure of MENT: evidence for functional loop-sheet polymers in chromatin condensation.","description":"Most serpins are associated with protease inhibition, and their ability to form loop-sheet polymers is linked to conformational disease and the human serpinopathies. Here we describe the structural and functional dissection of how a unique serpin, the non-histone architectural protein, MENT (Myeloid and Erythroid Nuclear Termination stage-specific protein), participates in DNA and chromatin condensation. Our data suggest that MENT contains at least two distinct DNA-binding sites, consistent with its simultaneous binding to the two closely juxtaposed linker DNA segments on a nucleosome. Remarkably, our studies suggest that the reactive centre loop, a region of the MENT molecule essential for chromatin bridging in vivo and in vitro, is able to mediate formation of a loop-sheet oligomer. Thes","dates":{"release":"2006-01-01T00:00:00Z","publication":"2006 Jul","modification":"2026-04-29T20:45:07.611Z","creation":"2019-03-27T01:45:36Z"},"accession":"S-EPMC1500978","cross_references":{"pubmed":["16810322"],"doi":["10.1038/sj.emboj.7601201"]}}