DC Field | Value | Language |
---|---|---|
dc.contributor.author | Holt, Matthew T. | ko |
dc.contributor.author | David, Yael | ko |
dc.contributor.author | Pollock, Sam | ko |
dc.contributor.author | Tang, Zhanyun | ko |
dc.contributor.author | Jeon, Jongcheol | ko |
dc.contributor.author | Kim, Jaehoon | ko |
dc.contributor.author | Roeder, Robert G. | ko |
dc.contributor.author | Muir, Tom W. | ko |
dc.date.accessioned | 2016-04-15T03:05:37Z | - |
dc.date.available | 2016-04-15T03:05:37Z | - |
dc.date.created | 2015-09-14 | - |
dc.date.created | 2015-09-14 | - |
dc.date.issued | 2015-08 | - |
dc.identifier.citation | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.112, no.33, pp.10365 - 10370 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.uri | http://hdl.handle.net/10203/203957 | - |
dc.description.abstract | Ubiquitylation of histone H2B at lysine 120 (H2B-Ub) plays a critical role in transcriptional elongation, chromatin conformation, as well as the regulation of specific histone H3 methylations. Herein, we report a strategy for the site-specific chemical attachment of ubiquitin to preassembled nucleosomes. This allowed expedited structure-activity studies into how H2B-Ub regulates H3K79 methylation by the methyltransferase human Dot1. Through an alanine scan of the ubiquitin surface, we identified a functional hotspot on ubiquitin that is required for the stimulation of human Dot1 in vitro. Importantly, this result was validated in chromatin from isolated nuclei by using a synthetic biology strategy that allowed selective incorporation of the hotspot-deficient ubiquitin mutant into H2B. The ubiquitin hotspot additionally impacted the regulation of ySet1-mediated H3K4 methylation but was not required for H2B-Ub-induced impairment of chromatin fiber compaction. These data demonstrate the utility of applying chemical ligation technologies to preassembled chromatin and delineate the multifunctionality of ubiquitin as a histone post-translational modification. | - |
dc.language | English | - |
dc.publisher | NATL ACAD SCIENCES | - |
dc.subject | HISTONE H2B | - |
dc.subject | HUMAN-CELLS | - |
dc.subject | H3K4 METHYLATION | - |
dc.subject | UBIQUITYLATION | - |
dc.subject | NUCLEOSOME | - |
dc.subject | DYNAMICS | - |
dc.subject | PROTEIN | - |
dc.subject | LEUKEMOGENESIS | - |
dc.subject | ACTIVATION | - |
dc.subject | EFFICIENT | - |
dc.title | Identification of a functional hotspot on ubiquitin required for stimulation of methyltransferase activity on chromatin | - |
dc.type | Article | - |
dc.identifier.wosid | 000359738300068 | - |
dc.identifier.scopusid | 2-s2.0-84940181324 | - |
dc.type.rims | ART | - |
dc.citation.volume | 112 | - |
dc.citation.issue | 33 | - |
dc.citation.beginningpage | 10365 | - |
dc.citation.endingpage | 10370 | - |
dc.citation.publicationname | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | - |
dc.identifier.doi | 10.1073/pnas.1504483112 | - |
dc.contributor.localauthor | Kim, Jaehoon | - |
dc.contributor.nonIdAuthor | Holt, Matthew T. | - |
dc.contributor.nonIdAuthor | David, Yael | - |
dc.contributor.nonIdAuthor | Pollock, Sam | - |
dc.contributor.nonIdAuthor | Tang, Zhanyun | - |
dc.contributor.nonIdAuthor | Roeder, Robert G. | - |
dc.contributor.nonIdAuthor | Muir, Tom W. | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | chromatin | - |
dc.subject.keywordAuthor | ubiquitin | - |
dc.subject.keywordAuthor | Dot1L | - |
dc.subject.keywordAuthor | epigenetics | - |
dc.subject.keywordAuthor | protein chemistry | - |
dc.subject.keywordPlus | HISTONE H2B | - |
dc.subject.keywordPlus | HUMAN-CELLS | - |
dc.subject.keywordPlus | H3K4 METHYLATION | - |
dc.subject.keywordPlus | UBIQUITYLATION | - |
dc.subject.keywordPlus | NUCLEOSOME | - |
dc.subject.keywordPlus | DYNAMICS | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | LEUKEMOGENESIS | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | EFFICIENT | - |
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