dc.contributor.author	Rahman, Nusrat
dc.contributor.author	Shamsuzzaman, Md
dc.contributor.author	Lindahl, Lasse
dc.date.accessioned	2021-06-29T21:41:38Z
dc.date.available	2021-06-29T21:41:38Z
dc.date.issued	2020-01-27
dc.description.abstract	Inhibition of the synthesis of an essential ribosomal protein (r-protein) abrogates the assembly of its cognate subunit, while assembly of the other subunit continues. Ribosomal components that are not stably incorporated into ribosomal particles due to the disrupted assembly are rapidly degraded. The 60S protein uL18/L5 is an exception and this protein accumulates extra-ribosomally during inhibition of 60S assembly. Since the r-proteins in each ribosomal subunit are essential only for the formation of their cognate subunit, it would be predicted that accumulation of extra-ribosomal uL18/L5 is specific to restriction of 60S assembly and does not occur abolition of 40S assembly. Contrary to this prediction, we report here that repression of 40S r-protein genes does lead to accumulation of uL18/L5 outside of the ribosome. Furthermore, the effect varies depending on which 40S ribosomal protein is repressed. Our results also show extra-ribosomal uL18/L5 is formed during 60S assembly, not during degradation of mature cytoplasmic 60S subunits. Finally, we propose a model for the accumulation of extra-ribosomal uL18 in response to the abolition of 40S r-proteins.	en_US
dc.description.sponsorship	This study was funded by grant number 0920578 from the National Science Foundation, USA to JM Zengel and LL, and a gift from The Benelein Technologies, LLC to LL (no grant number). Further funding was provided by an internal appropriation from the University of Maryland, Baltimore County to LL (no grant number). The funders had no role in study design, data collection, and analysis, decision to publish, or preparation of the manuscript.	en_US
dc.description.uri	https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0222479	en_US
dc.format.extent	6 files	en_US
dc.genre	journal articles	en_US
dc.identifier	doi:10.13016/m2wtkm-biqa
dc.identifier.citation	Rahman, Nusrat; Shamsuzzaman, Md; Lindahl, Lasse; Interaction between the assembly of the ribosomal subunits: Disruption of 40S ribosomal assembly causes accumulation of extra-ribosomal 60S ribosomal protein uL18/L5; PLOS ONE 15,1 , 27 January, 2020; https://doi.org/10.1371/journal.pone.0222479	en_US
dc.identifier.uri	https://doi.org/10.1371/journal.pone.0222479
dc.identifier.uri	http://hdl.handle.net/11603/21849
dc.language.iso	en_US	en_US
dc.publisher	PLOS	en_US
dc.relation.isAvailableAt	The University of Maryland, Baltimore County (UMBC)
dc.relation.ispartof	UMBC Biological Sciences Department Collection
dc.relation.ispartof	UMBC Faculty Collection
dc.rights	This item is likely protected under Title 17 of the U.S. Copyright Law. Unless on a Creative Commons license, for uses protected by Copyright Law, contact the copyright holder or the author.
dc.rights	Attribution 4.0 International (CC BY 4.0)	*
dc.rights.uri	https://creativecommons.org/licenses/by/4.0/	*
dc.title	Interaction between the assembly of the ribosomal subunits: Disruption of 40S ribosomal assembly causes accumulation of extra-ribosomal 60S ribosomal protein uL18/L5	en_US
dc.type	Text	en_US

Interaction between the assembly of the ribosomal subunits: Disruption of 40S ribosomal assembly causes accumulation of extra-ribosomal 60S ribosomal protein uL18/L5

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