The CTLH complex is a large, highly conserved eukaryotic complex composed of eight proteins that has been associated to several cellular functions, more often described as an E3 ubiquitin ligase complex involved in protein degradation through ubiquitination but also via vacuole-dependent degradation. A common feature observed in several components of this complex is the presence of the domains lissencephaly-1 homology (LisH) and C-terminal to LisH (CTLH). The LisH domain is found in several proteins involved in chromosome segregation, microtubule dynamics, and cell migration. Also, this domain participates in protein dimerization, besides affecting protein half-life, and influencing in specific cellular localization. Among the proteins found in the CTLH complex, Twa1 (Two-hybrid-associated protein 1 with RanBPM), also known as Gid8 (glucose-induced degradation protein 8 homolog) is the smallest, being a good model for structural studies by NMR. In this work we report the chemical shift assignments of the homodimeric LisH domain of Twa1, as a first step to determine its solution structure.
Homo sapiensChromosome segregation Ubiquitin ligase Dimerization Twa1 Gid8
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The Centro Nacional de Ressonância Magnética Nuclear Jiri Jonas (CNRMN-UFRJ) is gratefully acknowledged for providing access to NMR instrumentation. This work was supported by Fundação de Amparo à Pesquisa do Estado do Rio de Janeiro and Conselho Nacional de Desenvolvimento Científico e Tecnológico. We thank Jessica Moreira de Azevedo for technical support.
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