High impact information on DBP6

• Furthermore, coimmunoprecipitation and gel filtration analyses demonstrated that at least Npa2p, Dbp6p, Npa1p, Nop8p, and Rsa3p are present together in a subcomplex of low molecular mass whose integrity is independent of RNA [1].
• The rsa1 null allele synthetically enhances the mild growth defect of weak dbp6 alleles and confers synthetic lethality when combined with stronger dbp6 alleles [2].
• Dbp6p is an essential putative ATP-dependent RNA helicase that is required for 60S-ribosomal-subunit assembly in the yeast Saccharomyces cerevisiae (D. Kressler, J. de la Cruz, M. Rojo, and P. Linder, Mol. Cell. Biol. 18:1855-1865, 1998) [2].
• Dbp6p is essential for cell viability [3].
• In vivo depletion of Dbp6p results in a deficit in 60S ribosomal subunits and the appearance of half-mer polysomes [3].

Biological context of DBP6

• We propose that Dbp6p is required for the proper assembly of preribosomal particles during the biogenesis of 60S ribosomal subunits, probably by acting as an rRNA helicase [3].

Anatomical context of DBP6

• We conclude that Npa1p is required for ribosome biogenesis and operates in the same functional environment of Rsa3p and Dbp6p during early maturation of 60S ribosomal subunits [4].

Physical interactions of DBP6

• Moreover, Rsa3p is co-immunoprecipitated with protA-tagged Dbp6p under low salt conditions [5].

Other interactions of DBP6

• Synthetic lethality with conditional dbp6 alleles identifies rsa1p, a nucleoplasmic protein involved in the assembly of 60S ribosomal subunits [2].
• Both Dbp6p and Rsa3p are associated with complexes that most likely correspond to early pre-60S ribosomal particles [5].
• Altogether, our findings indicate an intimate functional interaction between Dbp6p and Dbp9p during the process of 60S-ribosomal-subunit assembly [6].

Analytical, diagnostic and therapeutic context of DBP6

• Furthermore, Dbp6p and Dbp9p weakly interact in a yeast two-hybrid assay [6].

References