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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 embryo, head explant

ABSTRACT: 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.

ORGANISM(S): Danio rerio

PROVIDER: GSE136003 | GEO | 2020/02/29

REPOSITORIES: GEO

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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

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

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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

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Rbm24 dictates mRNA recruitment for germ plasm assembly

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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.

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