The Intrinsically Disordered Regions of the Drosophila melanogaster Hox Protein Ultrabithorax Select Interacting Proteins Based on Partner Topology

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dc.citation.firstpagee108217en_US
dc.citation.issueNumber10en_US
dc.citation.journalTitlePLoS ONEen_US
dc.citation.volumeNumber9en_US
dc.contributor.authorHsiao, Hao-Chingen_US
dc.contributor.authorGonzalez, Kim L.en_US
dc.contributor.authorCatanese, Daniel J, Jr.en_US
dc.contributor.authorJordy, Kristopher E.en_US
dc.contributor.authorMatthews, Kathleen S.en_US
dc.contributor.authorBondos, Sarah E.en_US
dc.date.accessioned2015-01-06T19:20:34Zen_US
dc.date.available2015-01-06T19:20:34Zen_US
dc.date.issued2014en_US
dc.description.abstractInteractions between structured proteins require a complementary topology and surface chemistry to form sufficient contacts for stable binding. However, approximately one third of protein interactions are estimated to involve intrinsically disordered regions of proteins. The dynamic nature of disordered regions before and, in some cases, after binding calls into question the role of partner topology in forming protein interactions. To understand how intrinsically disordered proteins identify the correct interacting partner proteins, we evaluated interactions formed by the Drosophila melanogaster Hox transcription factor Ultrabithorax (Ubx), which contains both structured and disordered regions. Ubx binding proteins are enriched in specific folds: 23 of its 39 partners include one of 7 folds, out of the 1195 folds recognized by SCOP. For the proteins harboring the two most populated folds, DNA-RNA binding 3-helical bundles and α-α superhelices, the regions of the partner proteins that exhibit these preferred folds are sufficient for Ubx binding. Three disorder-containing regions in Ubx are required to bind these partners. These regions are either alternatively spliced or multiply phosphorylated, providing a mechanism for cellular processes to regulate Ubx-partner interactions. Indeed, partner topology correlates with the ability of individual partner proteins to bind Ubx spliceoforms. Partners bind different disordered regions within Ubx to varying extents, creating the potential for competition between partners and cooperative binding by partners. The ability of partners to bind regions of Ubx that activate transcription and regulate DNA binding provides a mechanism for partners to modulate transcription regulation by Ubx, and suggests that one role of disorder in Ubx is to coordinate multiple molecular functions in response to tissue-specific cues.en_US
dc.identifier.citationHsiao, Hao-Ching, Gonzalez, Kim L., Catanese, Daniel J, Jr., et al.. "The Intrinsically Disordered Regions of the Drosophila melanogaster Hox Protein Ultrabithorax Select Interacting Proteins Based on Partner Topology." <i>PLoS ONE,</i> 9, no. 10 (2014) Public Library of Science: e108217. http://dx.doi.org/10.1371/journal.pone.0108217.en_US
dc.identifier.doihttp://dx.doi.org/10.1371/journal.pone.0108217en_US
dc.identifier.urihttps://hdl.handle.net/1911/78896en_US
dc.language.isoengen_US
dc.publisherPublic Library of Scienceen_US
dc.rightsThis is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en_US
dc.titleThe Intrinsically Disordered Regions of the Drosophila melanogaster Hox Protein Ultrabithorax Select Interacting Proteins Based on Partner Topologyen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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