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SUMOylation is Required for Function of the Caenorhabditis elegans T-box Transcription Factor, TBX-2

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posted on 07.12.2012, 00:00 by Tanya L. Crum
T-box proteins are important dose-dependent developmental regulators of multicellular organisms, but little information exists regarding regulation of T-box factors in vivo. We are studying C. elegans TBX-2 to elucidate mechanisms controlling T-box factor function and regulation in animals. One way T-box factors may be regulated is through post-translational SUMOylation. SUMOylation is required for TBX-2 function. TBX-2 is SUMOylated in vitro and the minimal interaction domain between TBX-2 and SUMO-pathway components UBC-9 and GEI-17 was mapped. These interaction domains, TBX-2 LKIE and VKKE, match the classical SUMOylation consensus (ψKXD/E), and are necessary for SUMOylation of TBX-2. These interaction domains are likely UBC-9 and GEI-17 recruitment sites which may facilitate SUMOylation at other sites. TBX-2 and the C. elegans SUMO peptide, SMO-1, interact in vivo. Nuclear distribution and localization of the TBX-2/SMO-1 protein complex is dependent on the TBX-2 LKIE/VKKE interaction domain. UBC-9 depletion causes visual intensification of the subnuclear TBX-2 LKIE/VKKE mutant/SMO-1 BiFC signal. In addition, evidence demonstrating a strong genetic interaction between tbx-2 and ubc-9 and between tbx-2 and smo-1 in worms is provided.

History

Advisor

Schmidt, Jennifer V.

Department

Biological Sciences

Degree Grantor

University of Illinois at Chicago

Degree Level

Doctoral

Committee Member

Alfonso, Aixa Dubreuil, Ron Richmond, Janet E. Frolov, Maxim V.

Submitted date

2011-08

Language

en

Issue date

07/12/2012

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