LIM domain binding proteins 1 and 2 have different oligomeric states

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dc.contributor.authorCross, AJen_AU
dc.contributor.authorJeffries, CMen_AU
dc.contributor.authorTrewhella, Jen_AU
dc.contributor.authorMatthews, JMen_AU
dc.date.accessioned2010-08-02T04:30:40Zen_AU
dc.date.available2010-08-02T04:30:40Zen_AU
dc.date.issued2010-05-28en_AU
dc.date.statistics2010-05-28en_AU
dc.description.abstractLIM domain binding (Ldb) proteins are important regulators of LIM homeodomain and LIM-only proteins that specify cell fate in many different tissues. An essential feature of these proteins is the ability to self-associate, but there have been no studies that characterise the nature of this self-association. We have used deletion mutagenesis with yeast two-hybrid analysis to define the minimal self-association domains of Ldb1 and Ldb2 as residues 14–200 and 21–197, respectively. We then used a range of different biophysical methods, including sedimentation equilibrium and small-angle X-ray scattering to show that Ldb114–200 forms a trimer and Ldb221–197 undergoes a monomer–tetramer–octamer equilibrium, where the association in each case is of moderate affinity (105 M− 1). These modes of association represent a clear physical difference between these two proteins that otherwise appear to have very similar properties. The levels of association are more complex than previously assumed and emphasise roles of avidity and DNA looping in transcriptional regulation by Ldb1/LIM protein complexes. The abilities of Ldb1 and Ldb2 to form trimers and higher oligomers, respectively, should be considered in models of transcriptional regulation by Ldb1-containing complexes in a wide range of biological processes. © 2010, Elsevier Ltd.en_AU
dc.identifier.citationCross, A. J., Jeffries, C. M., Trewhella, J., & Matthews, J. M. (2010). LIM domain binding proteins 1 and 2 have different oligomeric states. Journal of Molecular Biology, 399(1), 133-144. doi:10.1016/j.jmb.2010.04.006en_AU
dc.identifier.govdoc2102en_AU
dc.identifier.issn0022-2836en_AU
dc.identifier.issue1en_AU
dc.identifier.journaltitleJournal of Molecular Biologyen_AU
dc.identifier.pagination133-144en_AU
dc.identifier.urihttp://dx.doi.org/10.1016/j.jmb.2010.04.006en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/1981en_AU
dc.identifier.volume399en_AU
dc.language.isoenen_AU
dc.publisherElsevieren_AU
dc.subjectSmall angle scatteringen_AU
dc.subjectProteinsen_AU
dc.subjectSedimentationen_AU
dc.subjectEquilibriumen_AU
dc.subjectBinding energyen_AU
dc.subjectTranscriptionen_AU
dc.titleLIM domain binding proteins 1 and 2 have different oligomeric statesen_AU
dc.typeJournal Articleen_AU
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