These authors contributed equally to this work.
Polypeptide chain release factor eRF3 is a novel molecular partner of survivin
Article first published online: 4 FEB 2013
© 2013 International Federation for Cell Biology
Cell Biology International
Volume 37, Issue 4, pages 359–369, April 2013
How to Cite
Xiao, R., Gao, Y., Shen, Q., Li, C., Chang, W. and Chai, B. (2013), Polypeptide chain release factor eRF3 is a novel molecular partner of survivin. Cell Biology International, 37: 359–369. doi: 10.1002/cbin.10043
- Issue published online: 11 MAR 2013
- Article first published online: 4 FEB 2013
- Accepted manuscript online: 17 JAN 2013 04:18AM EST
- Manuscript Accepted: 7 JAN 2013
- Manuscript Received: 31 OCT 2012
Additional supporting information may be found in the online version of this article.
|cbin10043-0001-sm-SupFig-S1.tif||99K||Figure S1. Expression and affinity purification of fusion proteins GST-heRF3b(lane 1 and 2), His-hSVV(lane 3 and 4), His-heRF3a-F3 (lane 5 and 6), and GST-hSVV (lane 7 and 8), and SDS–PAGE (10%) analysis of the fusion protein. The molecular weights of the proteins are ∼94.9, 17.2, 56.6 and 42.4 kDa, respectively.|
|cbin10043-0002-sm-SupFig-S2.tif||597K||Figure S2. N-terminal domain (NTD) sequence divergence of GSPT1 (eRF3a) and GSPT2 (eRF3b). GSPT1-1 and GSPT1-3 represent two isotypes of GSPT1. The dark-grey highlighted region represents the possible IAP-binding motif (Hegde et al., 2003); the arrow indicates the truncation site used to construct the mutant eRF3s. The yellow frame indicates the random coil secondary structure, whereas the red frame regions indicate α-helix secondary structure.|
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