Author: Cong, Yingying; Kriegenburg, Franziska; de Haan, Cornelis A. M.; Reggiori, Fulvio
Title: Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers Document date: 2017_7_18
ID: 15hzah62_8
Snippet: The S45 supernatant was also incubated with RNase A to degrade all nucleic acids ( Supplementary Fig. S1c ), before applying the sample onto the glycerol gradient to examine whether N protein oligomerization is influenced by binding to gRNA in vivo. This treatment, however, did not change the sedimentation profile of the N protein ( Fig. 2b and c). Altogether these data show that the MHV N protein forms large cytoplasmic oligomers in infected cel.....
Document: The S45 supernatant was also incubated with RNase A to degrade all nucleic acids ( Supplementary Fig. S1c ), before applying the sample onto the glycerol gradient to examine whether N protein oligomerization is influenced by binding to gRNA in vivo. This treatment, however, did not change the sedimentation profile of the N protein ( Fig. 2b and c). Altogether these data show that the MHV N protein forms large cytoplasmic oligomers in infected cells, and that this aggregation does not depend on its binding to gRNA. Moreover, this result underlines the validity of using recombinant N protein to study its oligomerization determinants.
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