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Coordinate regulation of ribosomal protein gene transcription mediates embryonic secretory cell growth

ABSTRACT: Coordinate regulation of ribosomal protein gene transcription mediates embryonic secretory cell growth

PROVIDER: PRJNA751749 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR15334164.fastq.gz	Fastqsanger.gz
	SRR15334165.fastq.gz	Fastqsanger.gz
	SRR15334166.fastq.gz	Fastqsanger.gz
	SRR15334167.fastq.gz	Fastqsanger.gz
	SRR15334168.fastq.gz	Fastqsanger.gz

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Coordinate regulation of ribosomal protein gene transcription mediates embryonic secretory cell growth

Project description:Cell growth is well defined for the late (post-embryonic) stages of development, but evidence for early (embryonic) cell growth during post-mitotic morphogenesis is quite limited. Here, we identify early cell growth as a key characteristic of Drosophila embryonic salivary gland (SG) tubulogenesis. A BTB/POZ domain nuclear factor, Ribbon (Rib), mediates early cell growth without affecting endoreplication. Rib binds the transcription start site of nearly every SG-expressed ribosomal protein gene (RPG), and is required for full expression of all RPGs tested. Rib binding to RPG enhancers is, however, weak and not sequence-specific, suggesting that specificity is achieved through co-factor interactions. We demonstrate Rib’s ability to physically interact with each of the three known activators of RPG transcription. Surprisingly, Rib-dependent early cell growth in another tubular organ—the embryonic trachea—is not mediated by direct RPG transcription. Our results support a model for tissue-specific transcriptional regulation in early cell growth programs.

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LARP1 senses free ribosomes to coordinate supply and demand of ribosomal proteins

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Project description:Terminal oligopyrimidine motif-containing (TOP) mRNAs encode all ribosomal proteins in mammals and are regulated to tune ribosome synthesis to cell state. Previous studies implicate LARP1 in 40S- or 80S-ribosome complexes that repress and stabilize TOP mRNAs. However, a mechanistic understanding of how LARP1 and TOP mRNAs interact with ribosomes to coordinate TOP mRNA outcomes is lacking. Here, we show that LARP1 senses the cellular supply of ribosomes by directly binding non-translating 80S ribosomes. Cryo-EM structures reveal a previously uncharacterized domain of LARP1 bound to and occluding the 40S mRNA channel and mutations at the LARP1-ribosome interface block formation of the 40S/80S-LARP1-TOP complexes. Free cytosolic ribosomes induce sequestration of TOP mRNAs in repressed 80S-LARP1-TOP complexes independent of alterations in mTOR signaling. Together, this work demonstrates a ribosome-sensing function of LARP1 that allows it to tune ribosome protein synthesis to the availability of free ribosomes.

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