| Autor: |
Vidhyadhar Nandana, Imalka W. Rathnayaka-Mudiyanselage, Nisansala S. Muthunayake, Ali Hatami, C. Bruce Mousseau, Luis A. Ortiz-Rodríguez, Jamuna Vaishnav, Michael Collins, Alisa Gega, Kaveendya S. Mallikaarachchi, Hadi Yassine, Aishwarya Ghosh, Julie S. Biteen, Yingxi Zhu, Matthew M. Champion, W. Seth Childers, Jared M. Schrader |
| Jazyk: |
angličtina |
| Rok vydání: |
2023 |
| Předmět: |
|
| Zdroj: |
Cell Reports, Vol 42, Iss 10, Pp 113229- (2023) |
| Druh dokumentu: |
article |
| ISSN: |
2211-1247 |
| DOI: |
10.1016/j.celrep.2023.113229 |
| Popis: |
Summary: Bacterial ribonucleoprotein bodies (BR-bodies) are non-membrane-bound structures that facilitate mRNA decay by concentrating mRNA substrates with RNase E and the associated RNA degradosome machinery. However, the full complement of proteins enriched in BR-bodies has not been defined. Here, we define the protein components of BR-bodies through enrichment of the bodies followed by mass spectrometry-based proteomic analysis. We find 111 BR-body-enriched proteins showing that BR-bodies are more complex than previously assumed. We identify five BR-body-enriched proteins that undergo RNA-dependent phase separation in vitro with a complex network of condensate mixing. We observe that some RNP condensates co-assemble with preferred directionality, suggesting that RNA may be trafficked through RNP condensates in an ordered manner to facilitate mRNA processing/decay, and that some BR-body-associated proteins have the capacity to dissolve the condensate. Altogether, these results suggest that a complex network of protein-protein and protein-RNA interactions controls BR-body phase separation and RNA processing. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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