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Rbm24 functions as a critical translational regulator to pretect crystallin proteins accumulation for lens transparency. RNA-seq data of 33 hpf rbm24a-/- and wildtype zebrafish embryo

ABSTRACT: Rbm24 functions as a critical translational regulator to pretect crystallin proteins accumulation for lens transparency. RNA-seq data of 33 hpf rbm24a-/- and wildtype zebrafish embryo

PROVIDER: PRJNA560932 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR10004223_1.fastq.gz	Fastqsanger.gz
	SRR10004223_2.fastq.gz	Fastqsanger.gz
	SRR10004224_1.fastq.gz	Fastqsanger.gz
	SRR10004224_2.fastq.gz	Fastqsanger.gz
	SRR10004225_1.fastq.gz	Fastqsanger.gz

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Rbm24 functions as a critical translational regulator to pretect crystallin proteins accumulation for lens transparency. RNA-seq data of 33 hpf rbm24a-/- and wildtype zebrafish embryo

Project description:This experiment is aimed to compare the transcriptomes of rbm24a mutant and wildtype at 33 hpf. As Rbm24a is an RNA binding protein, this comparation is suitable to obtain information on differential gene expression and alternative splicing. We found that the expression of most of the crystallin genes and many other lens specific genes are down regulated in rbm24a mutant, without changes in splicing patterns.

2020-02-29 | GSE136006 | GEO

Rbm24 functions as a critical translational regulator to pretect crystallin proteins accumulation for lens transparency. RNA-seq data of 33 hpf rbm24a-/- and wildtype embryo, head explant

2020-02-29 | GSE136003 | GEO

Rbm24 functions as a critical translational regulator to pretect crystallin proteins accumulation for lens transparency. RNA-seq data of 33 hpf rbm24a-/- and wildtype embryo, head explant

Project description:Rbm24 functions as a critical translational regulator to pretect crystallin proteins accumulation for lens transparency. RNA-seq data of 33 hpf rbm24a-/- and wildtype embryo, head explant

| PRJNA560923 | ENA

Analysis of mouse lens morphological and proteomic abnormalities following depletion of the betaB3-crystallin

Project description:Crystallin proteins serve as both essential structural and protective components of the ocular lens required for its transparency and light refraction. The mouse lens crystallin proteome is represented by alphaA-, alphaB-, betaA1-, betaA2-, betaA3-, betaA4-, betaB1-, betaB2-, betaB3-, gammaA-, gammaB-, gammaC-, gammaD-, gammaE, gammaF-, gammaN-, and gammaS-crystallin proteins encoded by 16 genes. Their mutations are responsible for lens opacification and early onset cataract formation. While many cataract-causing missense and nonsense mutations are known for these proteins, including the human CRYBB3 gene, the mammalian loss-of function model of the Crybb3 gene remains to be established. Herein, we generated the first mouse model via deletion of the Crybb3 promoter that abolished expression of the betaB3-crystallin resulting in disrupted lens morphology with initial phenotypic variability. The lens morphology was evaluated at histological levels and in-depth lens proteomes were analyzed using newborn, 3-week, 6-week, and 3-month-old lenses. These Crybb3-null lens proteomes showed both down- and up-regulation of various cytoplasmic and nuclear proteins with the largest differences found in 3-months lenses. Expression of Smarcc1/Baf155, b, and c proteins were validated by western immunoblotting/immunofluorescence. The betaB3-crystallin promoter region contain multiple binding sites of transcription factors AP-2a, c-Jun, c-Maf, Etv5, and Pax6, and is activated by FGF2 in cell culture experiments. Together, these studies establish the mouse Crybb3 loss-of-function model and its disrupted crystallin and non-crystallin proteomes.

2025-09-01 | PXD059220 | Pride

Disordered region encodes α-crystallin chaperone activity toward lens client γD-crystallin

Project description:Small heat-shock proteins (sHSPs) are a widely expressed family of ATP-independent molecular chaperones that are among the first responders to cellular stress. Mechanisms by which sHSPs delay aggregation of client proteins remain undefined. sHSPs have high intrinsic disorder content of up to ~60% and assemble into large, polydisperse homo- and hetero-oligomers, making them challenging structural and biochemical targets. Two sHSPs, HSPB4 and HSPB5, are present at millimolar concentrations in eye lens, where they are responsible for maintaining lens transparency over the lifetime of an organism. Together, HSPB4 and HSPB5 compose the hetero-oligomeric chaperone known as α-crystallin. To identify the determinants of sHSP function, we compared the effectiveness of HSPB4 and HSPB5 homo-oligomers and HSPB4/HSPB5 hetero-oligomers in delaying the aggregation of the lens protein γD-crystallin. In chimeric versions of HSPB4 and HSPB5, chaperone activity tracked with the identity of the 60-residue disordered N-terminal regions (NTR). A short 10-residue stretch in the middle of the NTR (“Critical sequence”) contains three residues that are responsible for high HSPB5 chaperone activity toward γD-crystallin. These residues affect structure and dynamics throughout the NTR. Abundant interactions involving the NTR Critical sequence reveal it to be a hub for a network of interactions within oligomers. We propose a model whereby the NTR critical sequence influences local structure and NTR dynamics that modulate accessibility of the NTR, which in turn modulates chaperone activity.

2023-01-31 | PXD035668 | Pride

rbm24a is an organizer component of germ plasm to determine germ cell fate

Project description:The formation of germ cells is a critical issue for the continuation of species. A large group of animals follow a preformation strategy to generate their primordial germ cells (PGCs). They produce a set of localized maternal mRNAs and proteins to form phase-separated germ plasm that functions as the PGC determinants, but the mechanisms underlying the assembly of germ plasm is poorly understood. This study identifies Rbm24a as an enssential localized germ plasm protein component that controls the formation of large and functional germ plasm granules. Rbm24a is complexed with Buc and interacts with germ plasm mRNAs, which determines the specific grasp of germ plasm mRNAs into the phase-separated aggregates. Rbm24a-absent granules fail to undergo kinesin-dependent transport towards the cleavage furrows, where small particles fuse into large ones. The loss of maternal rbm24a causes the complete degradation of germ plasm components and the disappearance of PGCs, resulting in totally sterile animals. Our work establishes that Rbm24 is a critical nucleating organizer component of germ plasm, highlighting an emerging common mechanism to read and recruit RNA component into phase-separated condensates.

2025-01-24 | GSE267406 | GEO

rbm24a is an organizer component of germ plasm to determine germ cell fate

2025-02-06 | GSE267086 | GEO

Murine lenses:βB2-crystallin W151C knock-in mice vs.wild type control mice

Project description:Transcriptional profiling of the lens in βB2-crystallin W151C mutation mice compared with wild type lenses

2023-02-21 | GSE225548 | GEO

rbm24a is an organizer component of germ plasm to determine germ cell fate (202409 validation)

2025-02-01 | GSE288109 | GEO

Nuclear Organization of Lens Epithelium and Fiber Cells in Newborn Lens

Project description:Cellular differentiation is marked by temporally and spatially coordinated gene expression regulated at multiple levels within the nucleus. Sequence-specific DNA-binding transcription factor CTCF EDIT. Topologically associated domains (TADs). Using Hi-C, we investigated changes in chromatin organization between newborn (P0.5) mouse lens fiber and epithelium and compared them to embryonic stem (ES) cells. Compartments A and B. Using ChIP-seq, we determined localization of CTCF in both lens tissues Formation of lens-specific TADs is demonstrated via comparative studies of chromatin at Pax6, Prox1, Gata3, Hsf4, and crystallin loci (to be updated) between lens and ES cell nuclei. Our study has generated the first data on nuclear organization in lens epithelium and lens fibers and directly compared these data with ES cells.

2023-10-16 | GSE243851 | GEO

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