Weidner, J. and Wang, C. and Prescianotto-Baschong, C. and Estrada, Al. F. and Spang, A.. (2014) The polysome-associated proteins Scp160 and Bfr1 prevent P body formation under normal growth conditions. Journal of Cell Science, 127 (5). pp. 1-35.
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Official URL: http://edoc.unibas.ch/dok/A6233713
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Abstract
Numerous mRNAs are degraded in processing bodies (P bodies) in S. cerevisiae. In logarithmically growing cells only 0-1 P bodies per cell are detectable. However, the number and appearance of P bodies change once the cell encounters stress. The polysome-associated mRNA binding protein Scp160 interacts with P body components such as the decapping protein Dcp2 and the scaffold protein Pat1, presumably on polysomes. Loss of either Scp160 or its interaction partner Bfr1 caused the formation of Dcp2-positive structures. These Dcp2-positive foci contained mRNA, since their formation was inhibited by the presence of cycloheximide. In addition, Scp160 was required for proper P body formation because only a subset of bona fide P body components could assemble into the Dcp2-positive foci in Δscp160 cells. In either Δbfr1 or Δscp160, P body formation was uncoupled from translational attenuation as the polysome profile remained unchanged. Collectively, our data suggest that Bfr1 and Scp160 prevent P body formation under normal growth conditions.
Faculties and Departments: | 05 Faculty of Science > Departement Biozentrum > Growth & Development > Biochemistry (Spang) |
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UniBasel Contributors: | Spang, Anne |
Item Type: | Article, refereed |
Article Subtype: | Research Article |
Publisher: | Company of Biologists |
ISSN: | 0021-9533 |
e-ISSN: | 1477-9137 |
Note: | Publication type according to Uni Basel Research Database: Journal article |
Language: | English |
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edoc DOI: | |
Last Modified: | 09 Nov 2017 13:16 |
Deposited On: | 27 Mar 2014 13:13 |
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