![]() To form the B* complex, U6-snRNA will then undergo conformational changes, forming its Internal Stem-Loop and a helix with U2-snRNA. ![]() It is also in this complex that the NTC and RBM22 arrive. In the B act Complex, U5-snRNA binds exonic sequences while U6-snRNA takes the place of U1 thus, the latter leaves the complex accompanied by U4-snRNP. The preformed tri-snRNP U4/U6.U5 then arrives on the complex, near the 5′-SS, to form the B Complex. U1 and U2-snRNAs first recognize specific sequences: U1 base-pairs with the 5′-splice site (5′-SS) and U2 base-pairs with the Branch Point (BP) sequence, forming Complex A. ZnF: Zinc Finger Domain RRM: RNA-Recognition Motif PRD: Proline-Rich Domain Aa: Amino acid.īrief scheme of pre-mRNA splicing. The α-helix 1 in the right panel corresponds to α-helix 9 in. For this representation, the structures are annotated in a N-ter to C-ter manner, from 1 to 4. This 2D representation aims at respecting as much as possible the adjacent structures, as described in. The aromatic residues of the RNP subdomains are represented by red dots. The latter presents an additional amino acid between the two aromatic residues of RNP1, and another α-helix between β 1 and α 1. Right panel shows the RRM of Cwc2, the yeast orthologue of RBM22. Left panel shows the consensus structure of the RRM. ![]() The structural homology between the three proteins suggests that RBM22 is a fusion gene of the two yeast genes ( C) Two-dimension representation of the structure of the RNA-Recognition Motif (RRM). The correspondence of exons with the domains of the protein is indicated, when known, with the grey dashed line between ( A) and ( B) ( B) Scheme of the domains of the human protein RBM22 and the two yeast proteins Cwc2 and Ecm2. Exons are represented by green and grey boxes when they are translated and are either in the 5′-UTR or 3′-UTR, respectively. RBM22 RBP RNA binding protein RRM motif alternative splicing cancer gene regulation myelodysplasia pre-mRNA splicing. RBM22 could represent a potential therapeutic target in specific diseases, and, notably, in cancer. Mutations, enforced expression level, and haploinsufficiency of RBM22 gene are observed in those diseases. Undoubtedly due to its wide scope in the regulation of gene expression, RBM22 has been associated with several pathologies and, notably, with the aggressiveness of cancer cells and with the phenotype of a myelodysplastic syndrome. RBM22 is also involved in gene regulation, and is able to bind DNA, acting as a bona fide transcription factor on a large number of target genes. RBM22 is mainly involved in pre-mRNA splicing, playing the essential role of maintaining the conformation of the catalytic core of the spliceosome and acting as a bridge between the catalytic core and other essential protein components of the spliceosome. RBM22 presents a Zinc Finger like and a Zinc Finger domain, an RNA-Recognition Motif (RRM), and a Proline-Rich domain with a general structure suggesting a fusion of two yeast genes during evolution: Cwc2 and Ecm2. This review focuses on RBM22, a gene encoding an RBP and belonging to the RNA-Binding Motif (RBM) family of genes. ![]() RNA-Binding Proteins (RBP) are very diverse and cover a large number of functions in the cells.
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