A role for the catalytic ribonucleoprotein RNase P in RNA polymerase III transcription

Reiner, Robert C.; Ben-Asouli, Yitzhak; Krilovetzky, Ilana; Jarrous, Nayef

doi:10.1101/gad.386706

Cited by 99 publications

(136 citation statements)

References 52 publications

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“…It is known that Rpp20 and Rpp25 have chromatin-binding capabilities. 40,41) Furthermore, the heterodimerization of Rpp20 and Rpp25 regulates their RNA-binding activity, subcellular localization, and expression. 19) A recent study showed that human nuclear RNase P is required for transcription of tRNA and other small noncoding RNA genes by pol III, and Rpp20 and Rpp25 are expected to play an essential role in this function as chromatin-binding proteins.…”

Section: Resultsmentioning

confidence: 99%

Crystal Structure and Functional Analysis of an Archaeal Chromatin Protein Alba from the Hyperthermophilic ArchaeonPyrococcus horikoshiiOT3

Hada

Nakashima

Osawa

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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Section: Resultsmentioning

confidence: 99%

Crystal Structure and Functional Analysis of an Archaeal Chromatin Protein Alba from the Hyperthermophilic ArchaeonPyrococcus horikoshiiOT3

Hada

Nakashima

Osawa

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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“…RNase P activity was shown (Reiner et al 2006) to coimmunoprecipitate with components of Pol III; depletion of RNase P resulted in significant reduction of the level of transcription of tRNA Tyr , tRNA Met , 5S rRNA, 7SL RNA, and U6 snRNA in HeLa cell extracts, and this effect was reversed by the addition of RNase P. Moreover, the knockdown of protein components of RNase P practically abolished Pol III transcription of 5S rRNA in whole HeLa cells. In addition, chromatin immunoprecipitation indicated that all analyzed protein components of RNase P associated with chromatin of actively transcribed, but not inactive, tRNA and 5S rRNA genes (Reiner et al 2006;Jarrous and Reiner 2007). A very similar effect of the presence of RNase P was recently reported for rRNA transcription by RNA polymerase I (Reiner et al 2008).…”

Section: Eukaryotic Rnase P In Transcriptionmentioning

confidence: 96%

Of proteins and RNA: The RNase P/MRP family

Esakova¹,

Krasilnikov²

2010

RNA

203

230

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Nuclear ribonuclease (RNase) P is a ubiquitous essential ribonucleoprotein complex, one of only two known RNA-based enzymes found in all three domains of life. The RNA component is the catalytic moiety of RNases P across all phylogenetic domains; it contains a well-conserved core, whereas peripheral structural elements are diverse. RNA components of eukaryotic RNases P tend to be less complex than their bacterial counterparts, a simplification that is accompanied by a dramatic reduction of their catalytic ability in the absence of protein. The size and complexity of the protein moieties increase dramatically from bacterial to archaeal to eukaryotic enzymes, apparently reflecting the delegation of some structural functions from RNA to proteins and, perhaps, in response to the increased complexity of the cellular environment in the more evolutionarily advanced organisms; the reasons for the increased dependence on proteins are not clear. We review current information on RNase P and the closely related universal eukaryotic enzyme RNase MRP, focusing on their functions and structural organization.

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“…RNase MRP is closely related to RNase P, but it has evolved to have a different specificity. RNase P is responsible for the 59-end maturation of tRNA and is involved in processing of other RNAs, including rRNA (Kazantsev and Pace 2006;Kirsebom 2007); RNase P was also shown to have a role in transcription (Reiner et al 2006). The vast majority of RNase MRP is located in the nucleolus (Kiss and Filipowicz 1992).…”

Section: Introductionmentioning

confidence: 99%

Footprinting analysis demonstrates extensive similarity between eukaryotic RNase P and RNase MRP holoenzymes

Esakova

Perederina²,

Quan

et al. 2008

RNA

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Eukaryotic ribonuclease (RNase) P and RNase MRP are evolutionary related RNA-based enzymes involved in metabolism of various RNA molecules, including tRNA and rRNA. In contrast to the closely related eubacterial RNase P, which is comprised of an RNA component and a single small protein, these enzymes contain multiple protein components. Here we report the results of footprinting studies performed on purified Saccharomyces cerevisiae RNase MRP and RNase P holoenzymes. The results identify regions of the RNA components affected by the protein moiety, suggest a role of the proteins in stabilization of the RNA fold, and point to substantial similarities between the two evolutionary related RNA-based enzymes.

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A role for the catalytic ribonucleoprotein RNase P in RNA polymerase III transcription

Abstract: Supplemental material is available at http://www.genesdev.org.

Cited by 99 publications

References 52 publications

Crystal Structure and Functional Analysis of an Archaeal Chromatin Protein Alba from the Hyperthermophilic ArchaeonPyrococcus horikoshiiOT3

Crystal Structure and Functional Analysis of an Archaeal Chromatin Protein Alba from the Hyperthermophilic ArchaeonPyrococcus horikoshiiOT3

Of proteins and RNA: The RNase P/MRP family

Footprinting analysis demonstrates extensive similarity between eukaryotic RNase P and RNase MRP holoenzymes

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