Yeast lariat debranching enzyme. Substrate and sequence specificity.
نویسندگان
چکیده
منابع مشابه
Metal dependence and branched RNA cocrystal structures of the RNA lariat debranching enzyme Dbr1.
Intron lariats are circular, branched RNAs (bRNAs) produced during pre-mRNA splicing. Their unusual chemical and topological properties arise from branch-point nucleotides harboring vicinal 2',5'- and 3',5'-phosphodiester linkages. The 2',5'-bonds must be hydrolyzed by the RNA debranching enzyme Dbr1 before spliced introns can be degraded or processed into small nucleolar RNA and microRNA deriv...
متن کاملStructural basis of lariat RNA recognition by the intron debranching enzyme Dbr1
The enzymatic processing of cellular RNA molecules requires selective recognition of unique chemical and topological features. The unusual 2',5'-phosphodiester linkages in RNA lariats produced by the spliceosome must be hydrolyzed by the intron debranching enzyme (Dbr1) before they can be metabolized or processed into essential cellular factors, such as snoRNA and miRNA. Dbr1 is also involved i...
متن کاملIdentification of the Specific Interactors of the Human Lariat RNA Debranching Enzyme 1 Protein
In eukaryotes, pre-mRNA splicing is an essential step for gene expression. We have been analyzing post-splicing intron turnover steps in higher eukaryotes. Here, we report protein interaction between human Debranching enzyme 1 (hDbr1) and several factors found in the Intron Large (IL) complex, which is an intermediate complex of the intron degradation pathway. The hDbr1 protein specifically int...
متن کاملA homolog of lariat-debranching enzyme modulates turnover of branched RNA.
Turnover of the branched RNA intermediates and products of pre-mRNA splicing is mediated by the lariat-debranching enzyme Dbr1. We characterized a homolog of Dbr1 from Saccharomyces cerevisiae, Drn1/Ygr093w, that has a pseudo-metallophosphodiesterase domain with primary sequence homology to Dbr1 but lacks essential active site residues found in Dbr1. Whereas loss of Dbr1 results in lariat-intro...
متن کاملSubstrate specificity of the gastrin-amidating enzyme.
As is the case with many other peptide hormones of the brain and gut, gastrin requires a carboxyl-terminal amide moiety for optimal biological activity. In the structure of progastrin, the carboxyl-terminal Phe of gastrin is followed by the sequence Gly93-Arg94-Arg95, which must be processed sequentially by an endoprotease, a carboxypeptidase, and an amidating enzyme to produce amidated bioacti...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1994
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)32037-9