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Resources » Paper

Welting TJ et al. (2006) RNA "Differential association of protein subunits with the human RNase MRP and RNase P complexes."

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  • Comments on Welting TJ et al. (2006) RNA "Differential association of protein subunits with the human RNase MRP and RNase P complexes." (0)

  • Overview

    PMID:
    16723659
    DOI:
    10.1261/rna.2293906
    Status:
    Publication type:
    Journal_article
    WormBase ID:
    WBPaper00028925

    Welting TJ, Kikkert BJ, van Venrooij WJ, & Pruijn GJ (2006). Differential association of protein subunits with the human RNase MRP and RNase P complexes. RNA, 12, 1373-82. doi:10.1261/rna.2293906

    RNase MRP is a eukaryotic endoribonuclease involved in nucleolar and mitochondrial RNA processing events. RNase MRP is a ribonucleoprotein particle, which is structurally related to RNase P, an endoribonuclease involved in pre-tRNA processing. Most of the protein components of RNase MRP have been reported to be associated with RNase P as well. In this study we determined the association of these protein subunits with the human RNase MRP and RNase P particles by glycerol gradient sedimentation and coimmunoprecipitation. In agreement with previous studies, RNase MRP sedimented at 12S and 60-80S. In contrast, only a single major peak was observed for RNase P at 12S. The analysis of individual protein subunits revealed that hPop4 (also known as Rpp29), Rpp21, Rpp20, and Rpp25 only sedimented in 12S fractions, whereas hPop1, Rpp40, Rpp38, and Rpp30 were also found in 60-80S fractions. In agreement with their cosedimentation with RNase P RNA in the 12S peak, coimmunoprecipitation with VSV-epitope-tagged protein subunits revealed that hPop4, Rpp21, and in addition Rpp14 preferentially associate with RNase P. These data show that hPop4, Rpp21, and Rpp14 may not be associated with RNase MRP. Furthermore, Rpp20 and Rpp25 appear to be associated with only a subset of RNase MRP particles, in contrast to hPop1, Rpp40, Rpp38, and Rpp30 (and possibly also hPop5), which are probably associated with all RNase MRP complexes. Our data are consistent with a transient association of Rpp20 and Rpp25 with RNase MRP, which may be inversely correlated to its involvement in pre-rRNA processing.


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