Cell
ArticleMultiple exon-binding sites in class II self-splicing introns
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Cryo-EM Structures of a Group II Intron Reverse Splicing into DNA
2019, CellCitation Excerpt :The RNA component of a group II intron is a ribozyme that has a conserved secondary structure with six domains (Lambowitz and Zimmerly, 2011; Figure S2). Domain I (DI) contains EBS1–EBS3 (Costa et al., 2000; Jacquier and Michel, 1987), used to target the group II intron to a specific DNA sequence. Domain IV (DIV) contains the open reading frame (ORF) for the maturase protein and provides the main binding site for the RT domain to form the fully assembled group II intron ribonucleoprotein (RNP) complex (Wank et al., 1999).
The role of Mg(II) in DNA cleavage site recognition in group II intron ribozymes: Solution structure and metal ion binding sites of the RNA·DNA complex
2014, Journal of Biological ChemistryCitation Excerpt :The EBS1·IBS1 interaction confers high specificity to the site of reinsertion of the intron, thus preventing insertion into sites from which the intron cannot splice again. However, it has been shown that EBS sequences are not conserved within different group II introns (17, 20, 21). For this reason, any desired sequence can be bound and cleaved by the intron in trans as long as the EBS and IBS sequences are complementary (22–25).
A 971-bp insertion in the rns gene is associated with mitochondrial hypovirulence in a strain of Cryphonectria parasitica isolated from nature
2011, Fungal Genetics and BiologyCitation Excerpt :A BLASTn search using the putative domain V sequence as a query also recovered several group II intron domain V sequences from fungi and plant mtDNA group II introns. Next to domain V, a sequence was detected that folds into domain VI, a domain that harbors the bulging adenine that provides a 2′ OH group for initiating a series of transesterification reactions that results in the splicing of the flanking exon sequences and the release of the intron RNA as a lariat (Costa et al., 2000; Jacquier and Michel, 1987; Kück et al., 1990; Lambowitz and Zimmerly, 2004; Michel et al., 1989, 2009; Schmelzer and Müller, 1987; Toor et al., 2001; van der Veen et al., 1986). The 5′ end of the intron starts with the characteristic GUGYG sequence (reviewed in Bonen and Vogel, 2001) and features such as the IBS1 and 2 and the corresponding EBS1 and 2 motifs (Bonen and Vogel, 2001; Michel et al., 1989) were also detected (Fig. 2).
The mechanism of splicing as told by group II introns: Ancestors of the spliceosome
2019, Biochimica et Biophysica Acta - Gene Regulatory MechanismsCitation Excerpt :Group II introns have conserved 5′ GUGYG sequences and 3′ AY end sequences, resembling the 5′ GU and 3′ AG sequences of spliceosomal introns [46]. Domain I (DI) is the largest domain at the 5′ end of the intron and contains sequences that base pair to exon sequences in order to align exon junctions at the active site for splicing and reverse splicing reactions [23,41,47]. These sequences consist of exon binding sequences (EBS) that recognize and bind intron binding sequences (IBS) in the exons and the δ nucleotide that binds the δ' nucleotide in DI (Fig. 2) [23,41,46,47].
Structural basis of branching during RNA splicing
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