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Functional characterization of Pwp2, a WD family protein essential for the assembly of the 90 S pre-ribosomal particle

AuthorsDosil, Mercedes ; Bustelo, Xosé R.
Issue Date2004
PublisherAmerican Society for Biochemistry and Molecular Biology
CitationJournal of Biological Chemistry 279(36): 37385-37397 (2004)
AbstractHere we report the functional characterization of Pwp2, an evolutionary conserved component of the 90 S pre-ribosome. Conditional depletion of the Pwp2 protein in yeast specifically impairs pre-rRNA proccessing at sites A 0, A1, and A2, leading to a strong decrease in 18 S rRNA and 40 S ribosomal subunit levels. Pre-ribosomal particle sedimentation analysis indicated that these defects are caused by a block in the formation of 90 S pre-ribosomes. We demonstrate that in Pwp2-depleted cells the U3 small necleolar ribonucleoprotein is not able to interact with the 35 S pre-rRNA and accumulates as a free complex. Similarly, other 90 S particle components such as Imp3 and Imp4 do not associate with the pre-rRNA precursor in the absence of Pwp2. In addition, we have found that after blocking U3 ribonucleoprotein assembly, Pwp2 predominantly accumulates as a complex in association with five proteins: Dip2, Utp6, Utp13, Utp18, and Utp21. Immunoprecipitation and gradient sedimentation analysis revealed that this Pwp2 small subcomplex is capable of interacting directly with the 35 S pre-rRNA 5′ end. Taken together, these results indicate that Pwp2 forms part of a stable particle subunit independent of the U3 small nucleolar ribonucleoprotein that is essential for the initial assembly steps of the 90 S pre-ribosome.
Identifiersdoi: 10.1074/jbc.M404909200
issn: 0021-9258
e-issn: 1083-351X
Appears in Collections:(IBMCC) Artículos
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