Conserved and variable domains of RNase MRP RNA

López, Marcela Dávila; Rosenblad, Magnus Alm; Samuelsson, Tore

doi:10.4161/rna.6.3.8584

Cited by 54 publications

(49 citation statements)

References 124 publications

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“…7D), one would expect to observe a phylogenetic conservation of key amino acids involved in this interaction; moreover, since the RNA interface involved in this interaction is well conserved from bacteria to eukaryotes (Chen and Pace 1997;Lopez et al 2009;Li et al 2011), one should expect a degree of similarity between phylogenetically conserved amino acids involved in interactions with RNA in bacterial RNase P and amino acids occupying equivalent spatial positions in eukaryotic (as well as in archaeal) Pop5. Indeed, a phylogenetic comparison of the sequences of the Figure 1A.…”

Section: Discussionmentioning

confidence: 99%

“…Yeast RNase MRP shares eight of its 10 protein components with RNase P (Chamberlain et al 1998;Walker et al 2010). The RNA component of RNase MRP (Lopez et al 2009) also shows clear similarities to the catalytic RNA component of RNase P; particularly, the secondary structure of the putative catalytic domain of RNase MRP closely resembles that of the catalytic domain of RNase P ( Fig. 1A,B; for a recent review, see Esakova and Krasilnikov 2010).…”

Section: Introductionmentioning

confidence: 99%

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Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP

Perederina

Khanova

Quan

et al. 2011

RNA

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Ribonuclease (RNase) MRP is a multicomponent ribonucleoprotein complex closely related to RNase P. RNase MRP and eukaryotic RNase P share most of their protein components, as well as multiple features of their catalytic RNA moieties, but have distinct substrate specificities. While RNase P is practically universally found in all three domains of life, RNase MRP is essential in eukaryotes. The structural organizations of eukaryotic RNase P and RNase MRP are poorly understood. Here, we show that Pop5 and Rpp1, protein components found in both RNase P and RNase MRP, form a heterodimer that binds directly to the conserved area of the putative catalytic domain of RNase MRP RNA. The Pop5/Rpp1 binding site corresponds to the protein binding site in bacterial RNase P RNA. Structural and evolutionary roles of the Pop5/Rpp1 heterodimer in RNases P and MRP are discussed.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP

Perederina

Khanova

Quan

et al. 2011

RNA

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“…1A,B; Esakova et al 2008 and references therein). Several nucleotides that are universally conserved in RNase P are also found in RNase MRP (Lopez et al 2009). Moreover, the P3 subdomains (Perederina et al 2010) of the two enzymes (Fig.…”

Section: Introductionmentioning

confidence: 99%

Substrate recognition by ribonucleoprotein ribonuclease MRP

Esakova

Perederina²,

Quan

et al. 2010

RNA

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The ribonucleoprotein complex ribonuclease (RNase) MRP is a site-specific endoribonuclease essential for the survival of the eukaryotic cell. RNase MRP closely resembles RNase P (a universal endoribonuclease responsible for the maturation of the 59 ends of tRNA) but recognizes distinct substrates including pre-rRNA and mRNA. Here we report the results of an in vitro selection of Saccharomyces cerevisiae RNase MRP substrates starting from a pool of random sequences. The results indicate that RNase MRP cleaves single-stranded RNA and is sensitive to sequences in the immediate vicinity of the cleavage site requiring a cytosine at the position +4 relative to the cleavage site. Structural implications of the differences in substrate recognition by RNases P and MRP are discussed.

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“…The RNA component of RNase MRP (Lopez et al 2009) contains a part closely resembling the catalytic domain of RNase P. This strongly suggests that, similar to RNase P, RNase MRP relies on its RNA moiety for catalysis (for re-1 view, see Esakova and Krasilnikov 2010). The protein composition of RNase MRP is also very similar to that of RNase P. S. cerevisiae RNase P has nine essential protein components: Pop1, Pop3, Pop4, Pop5, Pop6, Pop7, Pop8, Rpp1, and Rpr2 (for review, see Esakova and Krasilnikov 2010).…”

Section: Introductionmentioning

confidence: 99%

Structural organizations of yeast RNase P and RNase MRP holoenzymes as revealed by UV-crosslinking studies of RNA–protein interactions

Khanova¹,

Esakova²,

Perederina³

et al. 2012

RNA

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Eukaryotic ribonuclease (RNase) P and RNase MRP are closely related ribonucleoprotein complexes involved in the metabolism of various RNA molecules including tRNA, rRNA, and some mRNAs. While evolutionarily related to bacterial RNase P, eukaryotic enzymes of the RNase P/MRP family are much more complex. Saccharomyces cerevisiae RNase P consists of a catalytic RNA component and nine essential proteins; yeast RNase MRP has an RNA component resembling that in RNase P and 10 essential proteins, most of which are shared with RNase P. The structural organizations of eukaryotic RNases P/MRP are not clear. Here we present the results of RNA-protein UV crosslinking studies performed on RNase P and RNase MRP holoenzymes isolated from yeast. The results indicate locations of specific protein-binding sites in the RNA components of RNase P and RNase MRP and shed light on the structural organizations of these large ribonucleoprotein complexes.

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Conserved and variable domains of RNase MRP RNA

Cited by 54 publications

References 124 publications

Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP

Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP

Substrate recognition by ribonucleoprotein ribonuclease MRP

Structural organizations of yeast RNase P and RNase MRP holoenzymes as revealed by UV-crosslinking studies of RNA–protein interactions

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