Key result
The cloned human DBP2 gene localized to the nucleus and partially rescued the temperature-sensitive phenotype of S. pombe prp8 mutant cells, demonstrating it is a functional homolog.
DBP2 is identified as a functional human homolog of the fission yeast Cdc28/Prp8 protein, involved in pre-mRNA splicing.
Answers are grounded in this paper and cite their sources.
No immediate clinical implications; leaves open DBP2's role in human splicing disorders for further validation.
During the splicing process, spliceosomal snRNAs undergo numerous conformational rearrangements that appear to be catalyzed by proteins belonging to the DEAD/H-box superfamily of RNA helicases. We have cloned a new RNA helicase gene, designated DBP2 (DEAH-boxprotein), homologous to the Schizosaccaromyces pombe cdc28(+)/prp8(+) gene involved in pre-mRNA splicing and cell cycle progression. The full-length DBP2 contains 3400 nucleotides and codes for a protein of 1041 amino acids with a calculated mol. wt of 119 037 Da. Transfection experiments demonstrated that the GFP-DBP2 gene product, transiently expressed in HeLa cells, was localized in the nucleus. The DBP2 gene was mapped by FISH to the MHC region on human chromosome 6p21.3, a region where many malignant, genetic and autoimmune disease genes are linked. Because the expression of DBP2 gene in S.pombe prp8 mutant cells partially rescued the temperature-sensitive phenotype, we conclude that DBP2 is a functional human homolog of the fission yeast Cdc28/Prp8 protein.
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Osamu Imamura (1998) studied this question. The cloned human DBP2 gene localized to the nucleus and partially rescued the temperature-sensitive phenotype of S. pombe prp8 mutant cells, demonstrating it is a functional homolog.
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