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Lake water metagenome

ABSTRACT: Molecular investigation of protistan diversity along an elevation transect of alpine lakes using V9 SSU 18S

PROVIDER: PRJNA384345 | ENA |

REPOSITORIES: ENA

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Dataset's files

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			Action	DRS
	SRR5485120.fastq.gz	Fastqsanger.gz
	SRR5485130.fastq.gz	Fastqsanger.gz
	SRR5485140.fastq.gz	Fastqsanger.gz
	SRR5485150.fastq.gz	Fastqsanger.gz
	SRR5485121.fastq.gz	Fastqsanger.gz

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Effect of depletion of Sas10 in pre-rRNA processing

Project description:Ribosome small subunit (SSU) is assembled by the SSU processome which contains approximately 70 non-ribosomal protein factors. The biochemical mechanism for the SSU processome in 18S rRNA processing and maturation has been extensively studied, however, how the SSU processome components enter to the nucleolus has not been systematically investigated. Here we checked the nucleolar localization of 50 human SSU processome components and find that UTP3 and other 24 proteins enter to the nucleolus autonomously. For the remaining 25 proteins we find that UTP3/SAS10 assists the nucleolar localization of five proteins, namely MPP10, UTP25, EMG1 and two UTP-B components UTP12 and UTP13, and this ferry function of UTP3 is conserved in zebrafish. We also find that knockdown of human UTP3 impairs the cleavage at A0-site while loss-of-function of either utp3/sas10 or utp13/tbl3 in zebrafish causes an accumulation of the processed products containing the 5′ETS, supporting the crucial role of UTP3 in mediating the 5′ETS processing and degradation. Moreover, UTP3 directly interacts with and delivers EXOSC10 into the nucleolus, suggesting that UTP3 may play a direct role in recruiting the nuclear exosome to the SSU processome for degradation of the processed 5′ETS. These findings lay the ground for studying the mechanism of cytoplasm-to-nucleolus trafficking of the SSU processome components and the multifaceted roles of UTP3 during pre-rRNA processing.

2024-09-18 | GSE262698 | GEO

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