000206135 001__ 206135
000206135 005__ 20250730145425.0
000206135 0247_ $$2doi$$a10.1371/journal.pone.0096809
000206135 0247_ $$2WOS$$aWOS:000335728900099
000206135 0247_ $$2pmid$$apmid:24805353
000206135 0247_ $$2altmetric$$aaltmetric:2339661
000206135 0247_ $$2openalex$$aopenalex:W2008431787
000206135 037__ $$aPUBDB-2015-00661
000206135 041__ $$aEnglish
000206135 082__ $$a500
000206135 1001_ $$0P:(DE-H253)PIP1021020$$aKozlowska , Malgorzata$$b0
000206135 245__ $$aCalponin-Like Chd64 Is Partly Disordered
000206135 260__ $$aLawrence, Kan.$$bPLoS$$c2014
000206135 3367_ $$2DRIVER$$aarticle
000206135 3367_ $$2DataCite$$aOutput Types/Journal article
000206135 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1497593252_22659
000206135 3367_ $$2BibTeX$$aARTICLE
000206135 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000206135 3367_ $$00$$2EndNote$$aJournal Article
000206135 500__ $$3POF3_Assignment on 2016-02-15
000206135 500__ $$3POF3_Prefill: G:(DE-HGF)POF3-6215
000206135 500__ $$aOA
000206135 520__ $$a20-hydroxyecdysone (20E) and juvenile hormone (JH) signaling pathways interact to regulate insect development. Recently,two proteins, a calponin-like Chd64 and immunophilin FKBP39 have been found to play a pivotal role in the cross-talkbetween 20E and JH, although the molecular basis of interaction remains unknown. The aim of this work was to identify thestructural features that would provide understanding of the role of Chd64 in multiple and dynamic complex that cross-linksthe signaling pathways. Here, we demonstrate the results of in silico and in vitro analyses of the structural organization ofChd64 from Drosophila melanogaster and its homologue from Tribolium castaneum. Computational analysis predicted theexistence of disordered regions on the termini of both proteins, while the central region appeared to be globular, probablycorresponding to the calponin homology (CH) domain. In vitro analyses of the hydrodynamic properties of the proteinsfrom analytical size-exclusion chromatography and analytical ultracentrifugation revealed that DmChd64 and TcChd64 hadan asymmetrical, elongated shape, which was further confirmed by small angle X-ray scattering (SAXS). The Kratky plotindicated disorderness in both Chd64 proteins, which could possibly be on the protein termini and which would give rise tospecific hydrodynamic properties. Disordered tails are often involved in diverse interactions. Therefore, it is highly possiblethat there are intrinsically disordered regions (IDRs) on both termini of the Chd64 proteins that serve as platforms formultiple interaction with various partners and constitute the foundation for their regulatory function.
000206135 536__ $$0G:(DE-H253)POF2-P13-20130405$$aPETRA Beamline P13 (POF2-54G14)$$cPOF2-54G14$$fPOF II$$x0
000206135 693__ $$0EXP:(DE-H253)P-P13-20150101$$1EXP:(DE-H253)PETRAIII-20150101$$6EXP:(DE-H253)P-P13-20150101$$aPETRA III$$fPETRA Beamline P13$$x0
000206135 7001_ $$0P:(DE-H253)PIP1020427$$aTarczewska, Aneta$$b1
000206135 7001_ $$0P:(DE-HGF)0$$amichał, jakób$$b2
000206135 7001_ $$0P:(DE-H253)PIP1018895$$aSzpotkowski, Kamil$$b3
000206135 7001_ $$0P:(DE-H253)PIP1020216$$aWojtas, Magdalena$$b4
000206135 7001_ $$0P:(DE-HGF)0$$aAndrzej, Ozyhar$$b5$$eCorresponding author
000206135 773__ $$0PERI:(DE-600)2267670-3$$a10.1371/journal.pone.0096809$$n5$$pe96809$$tPLoS one$$v9$$x1932-6203$$y2014
000206135 8564_ $$uhttps://bib-pubdb1.desy.de/record/206135/files/Calponin-Like%20Chd64%20Is%20Partly%20Disordered.pdf$$yOpenAccess
000206135 8564_ $$uhttps://bib-pubdb1.desy.de/record/206135/files/Calponin-Like%20Chd64%20Is%20Partly%20Disordered.jpg?subformat=icon-1440$$xicon-1440$$yOpenAccess
000206135 8564_ $$uhttps://bib-pubdb1.desy.de/record/206135/files/Calponin-Like%20Chd64%20Is%20Partly%20Disordered.jpg?subformat=icon-180$$xicon-180$$yOpenAccess
000206135 8564_ $$uhttps://bib-pubdb1.desy.de/record/206135/files/Calponin-Like%20Chd64%20Is%20Partly%20Disordered.jpg?subformat=icon-640$$xicon-640$$yOpenAccess
000206135 8564_ $$uhttps://bib-pubdb1.desy.de/record/206135/files/Calponin-Like%20Chd64%20Is%20Partly%20Disordered.pdf?subformat=pdfa$$xpdfa$$yOpenAccess
000206135 909CO $$ooai:bib-pubdb1.desy.de:206135$$pdnbdelivery$$pdriver$$pVDB$$popen_access$$popenaire
000206135 9101_ $$0I:(DE-HGF)0$$6P:(DE-H253)PIP1021020$$aExternes Institut$$b0$$k>Extern
000206135 9101_ $$0I:(DE-HGF)0$$6P:(DE-H253)PIP1020427$$aExternes Institut$$b1$$k>Extern
000206135 9101_ $$0I:(DE-HGF)0$$6P:(DE-H253)PIP1018895$$aExternes Institut$$b3$$k>Extern
000206135 9101_ $$0I:(DE-HGF)0$$6P:(DE-H253)PIP1020216$$aExternes Institut$$b4$$k>Extern
000206135 9132_ $$0G:(DE-HGF)POF3-621$$1G:(DE-HGF)POF3-620$$2G:(DE-HGF)POF3-600$$9G:(DE-HGF)POF3-6215$$aDE-HGF$$bForschungsbereich Materie$$lVon Materie zu Materialien und Leben$$vIn-house research on the structure, dynamics and function of matter$$x0
000206135 9132_ $$0G:(DE-HGF)POF3-622$$1G:(DE-HGF)POF3-620$$2G:(DE-HGF)POF3-600$$9G:(DE-HGF)POF3-6G3$$aDE-HGF$$bForschungsbereich Materie$$lVon Materie zu Materialien und Leben$$vFacility topic: Research on Matter with Brilliant Light Sources$$x1
000206135 9131_ $$0G:(DE-HGF)POF2-54G14$$1G:(DE-HGF)POF2-540$$2G:(DE-HGF)POF2-500$$3G:(DE-HGF)POF2$$4G:(DE-HGF)POF$$9G:(DE-H253)POF2-P13-20130405$$aDE-H253$$bStruktur der Materie$$lForschung mit Photonen, Neutronen, Ionen$$vPETRA III$$x0
000206135 9141_ $$y2014
000206135 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection
000206135 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews
000206135 915__ $$0LIC:(DE-HGF)CCBY4$$2HGFVOC$$aCreative Commons Attribution CC BY 4.0
000206135 915__ $$0StatID:(DE-HGF)1040$$2StatID$$aDBCoverage$$bZoological Record
000206135 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR
000206135 915__ $$0StatID:(DE-HGF)0500$$2StatID$$aDBCoverage$$bDOAJ
000206135 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS
000206135 915__ $$0StatID:(DE-HGF)0111$$2StatID$$aWoS$$bScience Citation Index Expanded
000206135 915__ $$0StatID:(DE-HGF)0510$$2StatID$$aOpenAccess
000206135 915__ $$0StatID:(DE-HGF)9900$$2StatID$$aIF <  5
000206135 915__ $$0StatID:(DE-HGF)0310$$2StatID$$aDBCoverage$$bNCBI Molecular Biology Database
000206135 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline
000206135 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bThomson Reuters Master Journal List
000206135 9201_ $$0I:(DE-H253)EMBL-User-20120814$$kEMBL-User$$lEMBL-User$$x0
000206135 980__ $$ajournal
000206135 980__ $$aVDB
000206135 980__ $$aI:(DE-H253)EMBL-User-20120814
000206135 980__ $$aUNRESTRICTED
000206135 9801_ $$aFullTexts