Structural studies of a group I intron splicing factor and a continuous three-dimensional DNA lattice
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Loss of Chloroplast trnLUAA Intron in Two Species of Hedysarum (Fabaceae): Evolutionary Implications
Previous studies have indicated that in all land plants examined to date, the chloroplast gene trnLUAA isinterrupted by a single group I intron ranging from 250 to over 1400 bp. The parasitic Epifagus virginiana haslost, however, the entire gene. We report that the intron is missing from the chloroplast genome of twoarctic species of the legume genus Hedysarum (H. alpinum, H. ...
متن کاملStructural and biochemical analyses of DNA and RNA binding by a bifunctional homing endonuclease and group I intron splicing factor.
We determined the crystal structure of a bifunctional group I intron splicing factor and homing endonuclease, termed the I-AniI maturase, in complex with its DNA target at 2.6 A resolution. The structure demonstrates the remarkable structural conservation of the beta-sheet DNA-binding motif between highly divergent enzyme subfamilies. DNA recognition by I-AniI was further studied using nucleosi...
متن کاملA Tyrosyl-tRNA Synthetase Recognizes a Conserved tRNA-like Structural Motif in the Group I Intron Catalytic Core
The Neurospora crassa mitochondrial (mt) tyrosyl-tRNA synthetase (CYT-18 protein) functions in splicing group I introns, in addition to aminoacylating tRNA(Tyr). Here, we compared the CYT-18 binding sites in the N. crassa mt LSU and ND1 introns with that in N. crassa mt tRNA(Tyr) by constructing three-dimensional models based on chemical modification and RNA footprinting data. Remarkably, super...
متن کاملEvolution of RNA-Protein Interactions: Non-Specific Binding Led to RNA Splicing Activity of Fungal Mitochondrial Tyrosyl-tRNA Synthetases
The Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (mtTyrRS; CYT-18 protein) evolved a new function as a group I intron splicing factor by acquiring the ability to bind group I intron RNAs and stabilize their catalytically active RNA structure. Previous studies showed: (i) CYT-18 binds group I introns by using both its N-terminal catalytic domain and flexibly attached C-terminal antico...
متن کاملRestoration of correct splicing in IVSI-110 mutation of β-globin gene with antisense oligonucleotides: implications and applications in functional assay development
Objective(s): The use of antisense oligonucleotides (AOs) to restore normal splicing by blocking the recognition of aberrant splice sites by the spliceosome represents an innovative means of potentially controlling certain inherited disorders affected by aberrant splicing. Selection of the appropriate target site is essential in the success of an AO therapy. In this study, in search for a splic...
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تاریخ انتشار 2005