A G43 to U43 mutation in E. coli tRNATyrsu3+ which affects processing by RNase P

Furdon, Paul J.; Guerrier-Takada, Cecilia; Altman, Sidney

doi:10.1093/nar/11.5.1491

Cited by 19 publications

(14 citation statements)

References 29 publications

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“…RNase P activity has been initially defined as the activity responsible for the 59 maturation of tRNAs (Furdon et al 1983;Altman 2007). However, it has become evident that ribonucleoprotein RNase P enzymes in both prokaryotes and eukaryotes are involved in the maturation of a wide array of substrates; e.g., 4.5S RNA, tmRNA, viral RNAs, mRNAs, and riboswitches (e.g.…”

Section: Resultsmentioning

confidence: 99%

PRORP proteins support RNase P activity in both organelles and the nucleus in Arabidopsis

Gutmann¹,

Gobert²,

Giegé³

2012

Genes Dev.

120

167

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RNase P is an essential enzyme that cleaves the 59 leader sequence of tRNA precursors. RNase Ps were believed until now to occur universally as ribonucleoproteins in organisms performing RNase P activity. Here we find that protein-only RNase P enzymes called PRORP (for proteinaceous RNase P) support RNase P activity in vivo in both organelles and the nucleus in Arabidopsis. Beyond tRNA, PRORP proteins are involved in the maturation of small nucleolar RNA (snoRNA) and mRNA. Finally, ribonucleoprotein RNase MRP is not involved in tRNA maturation in plants. Altogether, our results indicate that ribonucleoprotein enzymes have been entirely replaced by proteins for RNase P activity in plants.Supplemental material is available for this article.Received February 10, 2012; revised version accepted April 5, 2012.RNase P is a virtually universal enzyme involved in the maturation of tRNAs, as it cleaves the 59 leader sequence of tRNA precursors. It is thus essential to obtain functional tRNAs and is therefore pivotal for translation (Lai et al. 2010;Reiter et al. 2010). RNase P activities from all phyla of life were assumed to be universally performed by ribonucleoprotein enzymes whose catalytic activities are held by ribozymes (Altman 2007). This concept was first challenged with the proposition that spinach chloroplast and human mitochondria RNase Ps would not contain any RNA moiety (Wang et al. 1988;Rossmanith and Karwan 1998). More recently, protein-only RNase P enzymes called PRORP (for proteinaceous RNase P) have been characterized at the molecular level in endosymbiotic organelles in both humans and Arabidopsis (Holzmann et al. 2008;Gobert et al. 2010). Still, the dogma remained that RNase P enzymes would nonetheless universally occur as ribonucleoproteins in living organisms performing RNase P activity, with protein-only RNase Ps being marginal exceptions restricted to only some organelles (e.g., Esakova and Krasilnikov 2010).The putative PRORP RNase P enzymes are characterized by the occurrence of a conserved ''NYN'' metallonuclease domain (Anantharaman and Aravind 2006). PRORP proteins also belong to the huge pentatricopeptide repeat (PPR) protein family. These proteins, typically from eukaryotes, are involved in a wide variety of posttranscriptional mechanisms (Schmitz-Linneweber and Small 2008). However, no functional information was available for PRORP proteins. We previously established that Arabidopsis PRORP1, a protein localized in organelles, can act in vitro as an RNase P enzyme that is a single protein (Gobert et al. 2010), although its function remained elusive in planta. We also used localization experiments (YFP fusions and immunodetections) to determine that PRORP2 and PRORP3, two paralogs of PRORP1, were present in Arabidopsis nuclei (Gobert et al. 2010). In addition, the fast-growing amount of genomic data has revealed that some important groups of eukaryotes, such as land plants and kinetoplastids, do not encode any recognizable genes for RNase P RNA or for proteins specific for ribonucleoprotein...

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Section: Resultsmentioning

confidence: 99%

PRORP proteins support RNase P activity in both organelles and the nucleus in Arabidopsis

Gutmann¹,

Gobert²,

Giegé³

2012

Genes Dev.

120

167

View full text Add to dashboard Cite

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“…The 5-leader sequences of precursors are removed by the action of an endonuclease, RNase P, which cleaves its substrates at a single site to generate the phosphorylated 5'-terminus of the mature tRNA. This reaction appears to be independent of the RNA base sequence at the site of cleavage but has been found to be sensitive to the secondary and tertiary structure of its substrates (1)(2)(3). The exact sequence of events along the tRNA maturation pathway in eukaryotes is not known, but the removal of 5-leader sequences appears to occur at an early stage.…”

Section: Intrquctionmentioning

confidence: 99%

Effects of tRNA-intron structure on cleavage of precursor tRNAs by RNase P fromSaccharomyces cerevisiae

Leontis¹,

DaLio²,

Strobel³

et al. 1988

Nucl Acids Res

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RNase P derived from S. cerevisiae nuclei was tested for its ability to cleave a variety of naturally occurring and selectively altered precursor-tRNA molecules to yield matured 5' termini. Precursors were synthesized in vitro in order to test which aspects of substrate structure are crucial to recognition and cleavage by RNase P. Base modifications in the precursor substrates are not required for cleavage by the enzyme, but deletion and substitution mutations affecting any portion of the precursor tertiary structure reduce cleavage. In particular, a number of alterations in the intervening sequence (IVS) reduce the susceptibility of the substrate to cleavage by RNase P. The significance of these results is discussed in reference to the contribution of the IVS to the structure of the precursor-tRNA.

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“…It must recognize mature tRNA sequences rather than precursor segments, since it correctly processes tRNAs with variable precursor sequences, including those from different species (2). Some modifications of the mature tRNA structure have been shown to result in delayed or inaccurate processing of the affected precursor (52,169). RNase P is not obligately the first or last step in tRNA maturation, since species with either mature or immature 3' ends are substrates for it.…”

Section: Small Rnasmentioning

confidence: 99%

Nucleolytic processing of ribonucleic acid transcripts in procaryotes.

King¹,

Sirdeskmukh²,

Schlessinger³

1986

Microbiological Reviews

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A G43 to U43 mutation in E. coli tRNATyrsu3+ which affects processing by RNase P

Cited by 19 publications

References 29 publications

PRORP proteins support RNase P activity in both organelles and the nucleus in Arabidopsis

PRORP proteins support RNase P activity in both organelles and the nucleus in Arabidopsis

Effects of tRNA-intron structure on cleavage of precursor tRNAs by RNase P fromSaccharomyces cerevisiae

Nucleolytic processing of ribonucleic acid transcripts in procaryotes.

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