Disease relevance of DBR1

• The hDBR1 cDNA expressed in Escherichia coli showed debranching activity in vitro and was also shown to be functional in an interspecies specific complementation experiment. hDBR1 cDNA in a S. cerevisiae expression vector complemented the intron accumulation phenotype of a S. cerevisiae dbr1 null mutant [1].

High impact information on DBR1

• In this work we report on a Dbr1p-dependent RNA decay pathway that limits the accumulation of splice-defective lariat intermediates stalled at the second step of splicing [2].
• In this pathway, splice-defective lariat intermediates are debranched by Dbr1p and subsequently degraded 5' to 3' primarily by the cytoplasmic exonuclease, Xrn1p [2].
• Frequency of TD was analyzed according to patients' sex, therapy scheme, HCV genotype and HLA DBR1 alleles [3].
• Integration of the cDNA for hDBR1 into the ura4 locus of S. pombe also complemented both the intron accumulation and slow growth phenotypes of a S. pombe dbr1 null mutant strain [1].
• Comparison of the amino acid sequence of hDBR1 with the other DBR protein sequences showed several conserved regions, with 40, 44 and 43% identity to the S. cerevisiae, S. pombe and C. elegans debranching enzymes, respectively [1].

References