Disease relevance of DBR1

• DBR1 siRNA inhibition of HIV-1 replication [1].

High impact information on DBR1

• The DBR1 gene has been isolated by complementation of the transposition phenotype [2].
• In dbr1 cells, excised introns derived from a variety of pre-mRNAs are remarkably stable and accumulate to levels exceeding that of the corresponding mRNA [2].
• Analysis of RNA extracted from a dbr1-delta strain, which lacks intron lariat-debranching activity, shows that U24 can be synthesized only from the debranched lariat [3].
• Yeast lariat debranching enzyme. Substrate and sequence specificity [4].
• Two other mutations, Y68F and Y68D, occur at a potential phosphorylation site, and we have shown that Dbr1p is phosphorylated on tyrosine [5].

Chemical compound and disease context of DBR1

• CONCLUSION: These data suggest that DBR1 function may be needed to debranch a putative HIV-1 genomic RNA lariat prior to completion of reverse transcription [1].

Biological context of DBR1

• Mapping of DBR1 and YPK1 suggests a major revision of the genetic map of the left arm of Saccharomyces cerevisiae Chromosome XI [6].
• Saccharomyces cerevisiae Dbr1 is a 405-amino acid RNA debranching enzyme that cleaves the 2'-5' phosphodiester bonds of the lariat introns formed during pre-mRNA splicing [7].
• Residues important for Dbr1 function include putative counterparts of the amino acids that comprise the active site of the metallophosphoesterase superfamily, exemplified by the DNA phosphodiesterase Mre11 [7].
• RESULTS: We designed three short interfering RNA (siRNA) molecules targeting DBR1, which were capable of reducing DBR1 mRNA expression by 80% and did not significantly affect cell viability [1].
• The RNA lariat debranching enzyme of mouse (mDBR1) was cloned by screening a NIH/3T3 cDNA library [8].

Associations of DBR1 with chemical compounds

• Structure-function analysis of yeast RNA debranching enzyme (Dbr1), a manganese-dependent phosphodiesterase [7].

Other interactions of DBR1

• Moreover, inactivation of the DBR1 gene in rrp2-1, or the RNT1 gene in rrp5-Delta3 mutant cells also negates the effects of the original mutation on pre-rRNA processing [9].
• Amongst 24 interacting clones isolated in a two-hybrid screening, seven could be identified as parts of the RAD2, RLF2 and DBR1 genes [10].
• Debranching this RNA in vitro with Dbr1p creates an uncapped version of the normal Ty1 RNA 5' end [11].

Analytical, diagnostic and therapeutic context of DBR1

• We used a mutagenic PCR method to generate a collection of dbr1 mutant alleles to explore the relationship between the roles of DBR1 in transposition and debranching [5].
• Cloning, expression, and complementation test of the RNA lariat debranching enzyme cDNA from mouse [8].

References