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RPL3L-containing ribosomes determine translation elongation dynamics required for cardiac function

ABSTRACT: RPL3L-containing ribosomes determine translation elongation dynamics required for cardiac function

PROVIDER: PRJNA838484 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR19217100.fastq.gz	Fastqsanger.gz
	SRR19217101.fastq.gz	Fastqsanger.gz
	SRR19217102.fastq.gz	Fastqsanger.gz
	SRR19217103.fastq.gz	Fastqsanger.gz
	SRR19217054.fastq.gz	Fastqsanger.gz

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RPL3L-containing ribosomes determine translation elongation dynamics required for cardiac function

Project description:Although several ribosomal protein (RP) paralogs are expressed in a tissue-specific manner, how these proteins affect translation and why they are required only in certain tissues have remained unclear. Here we show that RPL3L, a paralog of RPL3 specifically expressed in heart and skeletal muscle, influences translation elongation dynamics. Deficiency of RPL3L-containing ribosomes (RPL3L-ribosomes) in RPL3L knockout male mice resulted in impaired cardiac contractility. Ribosome occupancy at mRNA codons was found to be altered in the RPL3L-deficient heart, and the changes were negatively correlated with those observed in myoblasts overexpressing RPL3L. RPL3L-ribosomes were less prone to collisions compared with RPL3-containing canonical ribosomes. Although the loss of RPL3L-ribosomes altered translation elongation dynamics for the entire transcriptome, its effects were most pronounced for transcripts related to cardiac muscle contraction and dilated cardiomyopathy, with the abundance of the encoded proteins being correspondingly decreased. Our results provide new insight into the mechanisms and physiological relevance of tissue-specific translational regulation.

2023-03-15 | GSE203072 | GEO

RPL3L-containing ribosomes determine translation elongation dynamics required for cardiac function.

Project description:Although several ribosomal protein paralogs are expressed in a tissue-specific manner, how these proteins affect translation and why they are required only in certain tissues have remained unclear. Here we show that RPL3L, a paralog of RPL3 specifically expressed in heart and skeletal muscle, influences translation elongation dynamics. Deficiency of RPL3L-containing ribosomes in RPL3L knockout male mice resulted in impaired cardiac contractility. Ribosome occupancy at mRNA codons was found to be altered in the RPL3L-deficient heart, and the changes were negatively correlated with those observed in myoblasts overexpressing RPL3L. RPL3L-containing ribosomes were less prone to collisions compared with RPL3-containing canonical ribosomes. Although the loss of RPL3L-containing ribosomes altered translation elongation dynamics for the entire transcriptome, its effects were most pronounced for transcripts related to cardiac muscle contraction and dilated cardiomyopathy, with the abundance of the encoded proteins being correspondingly decreased. Our results provide further insight into the mechanisms and physiological relevance of tissue-specific translational regulation.

| S-EPMC10119107 | biostudies-literature

Mammalian heart RPL3L

Project description:RPL3L-containing ribosomes modulate mitochondrial activity in the mammalian heart.

| PRJEB49255 | ENA

Characterizing role of striated-muscle specific ribosomal protein L3-like (Rpl3L) in mouse hearts

Project description:Overall goal: To elucidate the function served by Rpl3L in heart. Purpose of analysis: To determine effects of Rpl3L-deficiency on translational mRNA profile in heart. Experimental structure: Polysomes and monosomes were fractionated from cardiac ventricles and associated RNA extracted for library generation and differential gene expression analyses between wild-type and Rpl3L-null samples, using standard RNAseq pipeline.

2023-02-10 | GSE215869 | GEO

Defining the effects of Rpl3L-deficiency on transcriptional profiles of mouse hearts

Project description:The ribosomal protein L3-like (RPL3L) is a striated muscle-specific ribosomal protein, and mutations in human RPL3L are linked with childhood cardiomyopathy and age-related atrial fibrillation. However, the function served by this protein, a paralogue of the ubiquitously expressed RPL3 protein, remains poorly characterized in both heart and skeletal muscle. To address this, null mutant mice with the Rpl3L gene deleted were generated and studied. The purpose of this microarray analyses was to compare transcriptional profiles of the null mutant hearts (lacking RPL3L) with wild-type control hearts (expressing RpL3L). We used microarrays to elucidate effects of Rpl3L deficiency on transcriptional profile of mouse hearts

2023-02-10 | GSE216168 | GEO

Translation elongation factor 4 (LepA) contributes to tetracycline susceptibility by stalling elongating ribosomes

Project description:Purpose: We use the ribosome profiling protocol to understand EF4 mediated translation events. Methods: We used ribosome profiling data to analyze by plastid software. The ribosome were purified by sucrose gradient separation. Results: Using sequencing data, we found that EF4 mediates the 1-nucleotide conformational change of ribosomes. We also found that many genes involved in translation after tetracycline treatment. Finally, we found that EF4 stalls the elongating ribosomes globally. Conclusions: Our results suggest that EF4 mediates both 30S biogenesis and translation elongation process, in particular, EF4 stalls the elongating ribosomes globally.

2018-05-14 | GSE106448 | GEO

Nano-TRAP Input and IP sequencing of WT and Rpl3l-/- mouse hearts

Project description:RPL3L is a ribosomal protein expressed exclusively in adult straited muscle tissues, and a paralogue of the ubiquitously expressed RPL3. Here, we are looking into the effects of Rpl3l knockout on translation in adult mice hearts.

2022-05-16 | GSE189872 | GEO

Ribo-Seq and RNA-seq sequencing of WT and Rpl3l-/- mouse hearts

2022-05-16 | GSE189854 | GEO

The role of Rpl3l in translation in cardiomyocytes

Project description:Ribosome immunoprecipitates of cardiomyocytes isolated from Rpl3l-/- and Rpl3l+/+ mouse hearts were analysed using mass spectrometry.

2023-03-08 | PXD026985 | Pride

eIF3 associates with 80S ribosomes to promote translation elongation, mitochondrial homeostasis, and muscle health

Project description:eIF3 is a multi-subunit complex thought to execute numerous functions in canonical translation initiation, including mRNA recruitment to the 40S ribosome, scanning for the start codon, and inhibition of 60S subunit joining 1–3. eIF3 was also found to interact with 40S and 60S ribosomal proteins and translation elongation factors 4, but a direct involvement in translation elongation has never been demonstrated. Using selective ribosome profiling, we made the unexpected observation that eIF3 remains bound to post-initiation 80S ribosomes, followed by release after translation of ~50 codons. Furthermore, eIF3 deficiency reduces early ribosomal elongation speed, particularly on mRNAs encoding proteins associated with membrane-associated functions, resulting in defective synthesis of their encoded proteins and abnormal mitochondrial and lysosomal physiology. Accordingly, heterozygous eIF3e+/- knockout mice accumulate giant mitochondria in skeletal muscle and show a progressive decline in muscle strength with age. Hence, in addition to its canonical role in translation initiation, eIF3 interacts with 80S ribosomes to enhance, at the level of early elongation, the synthesis of proteins with membrane-associated functions, an activity that is critical for normal muscle health.

2020-06-15 | GSE149697 | GEO

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