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Elucidating the structure and function of the β-propeller of Erb1 in the context of Nop7-Erb1-Ytm1 complex

AutorWegrecki, Marcin ; Rodríguez-Galán, Olga ; de la Cruz, Jesús; Bravo, Jerónimo
Fecha de publicación19-ago-2015
CitaciónEMBO Conference: Ribosome synthesis Brussels, Belgium (2015)
ResumenAlthough it has been proposed that the C-terminal WD40 domain of Erb1 is dispensable for Nop7-Erb1-Ytm1 trimer assembly, here we show the crystal structure of the dimer formed by full-length Ytm1 bound to the β-propeller domain of Erb1 from Chaetomium thermophilum (ChYtm1 and ChErb1432-801 respectively). The structural findings have been confirmed in vitro using affinity co-purification, gel filtration, interferometry and ITC. Generation of a mutant β-propeller of ChErb1 that binds ChYtm1 less efficiently further evidences its importance in the dimer formation. Moreover, we prove that an analogous mutation affects ribosome biogenesis in yeast.
DescripciónPóster presentado a EMBO Conference: Ribosome synthesis Brussels, Belgium. 19 – 23 August 2015
URIhttp://hdl.handle.net/10261/124657
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