نتایج جستجو برای: group i intron
تعداد نتایج: 1933205 فیلتر نتایج به سال:
The yeast mitochondrial group I intron b15 undergoes self-splicing at high Mg2+ concentrations, but requires the splicing factor CBP2 for reaction under physiological conditions. Chemical accessibility and UV cross-linking experiments now reveal that self-processing is slow because functional elements are not properly positioned in an active tertiary structure. Folding energy provided by CBP2 d...
Riboswitches are mRNA-based elements that regulate gene expression via binding of a specific ligand. Breaker and coworkers have now discovered a novel type of regulatory RNA motif that acts by c-di-GMP-dependent control of a self-splicing group I intron ribozyme (Lee et al., 2010).
resistance to qoi fungicide and cytochrome b diversity in the hungarian botrytis cinerea population
quinol oxidation inhibitors (qois) are one of the most important classes of fungicides used in agriculture. they block electron transfer between cytochrome b and cytochrome c1, thereby impeding the production of atp via oxidative phosphorylation. qoi fungicides are generally at high risk of provoking resistance in fungal phytopathogens. resistance has been reported in more than thirty species, ...
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...
We report the 3.4 angstrom crystal structure of a catalytically active group I intron splicing intermediate containing the complete intron, both exons, the scissile phosphate, and all of the functional groups implicated in catalytic metal ion coordination, including the 2'-OH of the terminal guanosine. This structure suggests that, like protein phosphoryltransferases, an RNA phosphoryltransfera...
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