ライフサイエンスコーパス: RNase P

1 of conserved nucleobases in ribonuclease P (RNase P).

2 ty that is hidden in cellular substrates for RNase P.

3 iple proteins, most of which are shared with RNase P.

4 ion and cleavage of a tRNA-like structure by RNase P.

5 bserved in cells deficient for mitochondrial RNase P.

6 observed with partially purified native Mma RNase P.

7 d a discussion of some research prospects on RNase P.

8 uggest a universal mechanism of catalysis by RNase P.

9 inity Mg(II) activates cleavage catalyzed by RNase P.

10 the environment of an essential metal ion in RNase P.

11 orresponding to G378 and G379 in B. subtilis RNase P.

12 l model for finding other potential roles of RNase P.

13 served and essential for tRNA recognition by RNase P.

14 that contributes to molecular recognition of RNase P.

15 ocessing of mitochondrial precursor tRNAs by RNase P.

16 cleolytic processing was solely dependent on RNase P.

17 RNAs that subsequently become substrates for RNase P.

18 in subunit shared by archaeal and eukaryotic RNase P.

19 iating the role of multiple Rpps in archaeal RNase P.

20 Rpp29 is a protein subunit of RNase P.

21 plex and larger endogenous ribonucleoprotein RNase P.

22 overy of antibacterial compounds that target RNase P.

23 fied as a new inhibitor of Bacillus subtilis RNase P.

24 stinguishes them from bacterial and archaeal RNases P.

25 Augmented import of RNase P, 5S rRNA, and MRP RNAs depended on PNPASE expres

26 Ribonuclease P (RNase P), a ribonucleoprotein (RNP) complex required for

27 NA and recruit intracellular ribonuclease P (RNase P), a tRNA processing enzyme, to degrade target mR

28 ns, we now add L7Ae as a subunit of archaeal RNase P, a ribonucleoprotein (RNP) that catalyzes 5'-mat

29 lso been identified as a subunit of archaeal RNase P, a ribonucleoprotein complex that employs an RNA

30 RNase P, a ribonucleoprotein enzyme that catalyzes the r

31 render the mRNA susceptible to hydrolysis by RNase P, a tRNA processing enzyme.

32 Knockdown of RNase P abolishes the assembly of initiation complexes b

33 cular composition, the RNA and protein-based RNase P act as dynamic scaffolds for the binding and pos

34 ure of how metals coordinate to the putative RNase P active site in solution, and shed light on the e

35 n which it can provide organellar or nuclear RNase P activities.

36 of RNase P, we developed the first real-time RNase P activity assay using fluorescence polarization/a

37 ed that N. equitans does not have or require RNase P activity because it lacks 5' tRNA leaders.

38 The large stimulatory effect of Mma L7Ae on RNase P activity decreases to <or= 4% of wild type upon

39 h a chimeric RNase P as their sole source of RNase P activity exhibit extremely variable responses.

40 The protein has RNase P activity in vitro and rescued the growth of Esch

41 rotein subunits are associated with archaeal RNase P activity in vivo: RPP21, RPP29, RPP30, and POP5.

42 essential for efficient Thermotoga maritima RNase P activity.

43 lly purified Methanococcus maripaludis (Mma) RNase P activity.

44 e P RNA maturation, which positively affects RNase P activity.

45 a and most Bacteria also encode an RNA-based RNase P; activity of both RNase P forms from the same ba

46 contains a nucleotide at N(-4) that enhances RNase P affinity.

47 Bacterial RNase P also processes precursor 4.5S RNA, tmRNA, 30S pr

48 The chimeric RNase P alters growth rates-used here as an indirect mea

49 l component of mitochondrial Ribonuclease P (RNase P), an enzyme required for mitochondrial tRNA proc

50 We investigated Pyrococcus furiosus (Pfu) RNase P, an archaeal RNP that catalyzes tRNA 5' maturati

51 Furthermore, RNase P, an endoribonuclease that normally generates the

52 RNA substrates including tRNA precursors for RNase P and 5.8 S rRNA precursors, as well as some mRNAs

53 (snoRNAs), because these both copurify with RNase P and accumulate larger forms in the RNase P tempe

54 t 1) and MEN beta, are formed by cleavage by RNase P and are capped but not polyadenylated.

55 atomic-level information on the mechanism of RNase P and continue to expand our understanding of the

56 codes for a protein subunit of mitochondrial RNase P and has another unknown essential function.

57 mmon RNA-mediated catalytic mechanism in all RNase P and help uncover parallels in RNase P catalysis

58 nces of pre-tRNAs may be common in bacterial RNase P and may lead to species-specific substrate recog

59 key subunits of the human endoribonucleases RNase P and MRP.

60 standing of the function and organization of RNase P and MRP.

61 and image processing we show that eukaryotic RNase P and RNase MRP have a modular architecture, where

62 The structures of RNase P and RNase MRP have not yet been solved, so it is

63 Pop6, and Pop7 proteins, known components of RNase P and RNase MRP, bind to yeast telomerase RNA and

64 lso the sites of greatest difference between RNase P and RNase MRP, highlighting the importance of th

65 maintenance of the MRPP1-HSD10 subcomplex of RNase P and that loss of HSD10 causes impaired mitochond

66 genously expressed non-coding RNAs: 5S rRNA, RNase P and the btuB riboswitch.

67 ogous to those of the J11/12-J12/11 motif of RNase P and the L1 stalk of the ribosomal E-site.

68 bles the D- and T-loop binding elements from RNase P and the ribosome exit site, suggesting that this

69 Ribonuclease P (RNase P) and RNase MRP are closely related ribonucleopro

70 t is closely related to the RNA component of RNase P, and multiple proteins, most of which are shared

71 RNase P appears to participate in the splicing-independe

72 s for Bacillus subtilis and Escherichia coli RNase P are enhanced by sequence-specific contacts betwe

73 suggesting that rates of ptRNA processing by RNase P are tuned for uniform specificity and consequent

74 proK and proM transcripts, while PNPase and RNase P are utilized in the processing of proL The termi

75 The card also includes human RNase P as a nucleic acid extraction control and an inte

76 coli cells forced to survive with a chimeric RNase P as their sole source of RNase P activity exhibit

77 In this study, we constructed a functional RNase P-based ribozyme (M1GS RNA) that targets the overl

78 owed that Salmonella can efficiently deliver RNase P-based ribozyme sequence in specific human cells,

79 RNomic studies have shown that RNase P binds other RNAs in addition to tRNAs, but no no

80 entarity with a target RNA and the action of RNase P, but also to a non-gene-specific tight binding o

81 makes the latter a substrate for endogenous RNase P by rendering the bipartite target RNA-EGS comple

82 in all RNase P and help uncover parallels in RNase P catalysis hidden by plurality in its subunit mak

83 able mechanisms by which L7Ae contributes to RNase P catalysis.

84 nctional group modifications of U51 decrease RNase P-catalyzed phosphodiester bond cleavage 16- to 23

85 RNase P catalyzes the Mg(2)(+)-dependent 5'-maturation o

86 Bacterial ribonuclease P (RNase P) catalyzes the cleavage of 5' leader sequences f

87 Ribonuclease P (RNase P) catalyzes the maturation of the 5' end of tRNA

88 ata are the first evidence that defective mt:RNase P causes mitochondrial dysfunction, lethality and

89 The EGS variant induced human RNase P cleavage of ICP4 mRNA sequence 60 times better t

90 l be discussed using a model where bacterial RNase P cleavage proceeds through a conformational-assis

91 at the site immediately 5' of the canonical RNase P cleavage site, the -1 position, to study Escheri

92 ch mature 5' terminus is generated by single RNase P cleavage, while the 3' terminus undergoes exonuc

93 The 3'-end of Men beta is generated by RNase P cleavage.

94 Rather, RNase P cleavages separate the individual tRNA precursor

95 RNase P cleaves 4-7 nt downstream of the CCA determinant

96 In this study, we found that RNase P cleaves OLE RNA and that the cleavage leads to a

97 Endogenous RNase P cleaves the mRNA in the complex, making it inact

98 RNase P cleaves the nascent MALAT1 transcript downstream

99 We also show that archaeal and eukaryal RNase P, compared to their bacterial relatives, exhibit

100 PP30), we show that addition of L7Ae to this RNase P complex increases the optimal reaction temperatu

101 As part of the ribonucleoprotein RNase P complex, the RNA component catalyzes essential r

102 3, form the mitochondrial ribonuclease P (mt-RNase P) complex that cleaves the 5' ends of mt-tRNAs fr

103 Bacillus subtilis ribonuclease P (RNase P), composed of a catalytically active RNA subunit

104 Archaeal RNase P comprises an RPR and at least four RPPs, which h

105 Typical RNase P consists of a catalytic RNA component and a prot

106 RNase P consists of three different proteins MRPP1, MRPP

107 Our results imply that RNase P could play a role in the regulation of gene expr

108 Under RNase P-deficient conditions, the amount of OLE RNA incr

109 First, RNase P-dependant changes in RNA abundance were examined

110 cRNAs NEAT1, MALAT1, and RPPH1, composing an RNAse P-dependent lncRNA-maturation pathway, were also u

111 m the H1 RNA, the RNA component of the human RNase P enzyme, appended to a nonimported RNA directs th

112 functional RNP intermediates en route to the RNase P enzyme, but provided no information on subunit s

113 ctionally conserved protein component of the RNase P enzyme.

114 NA complex that illustrates how protein-only RNase P enzymes specifically bind tRNA and highlights th

115 Until recently, all identified RNase P enzymes were a ribonucleoprotein with a conserve

116 jugates as selective inhibitors of bacterial RNase P, especially once the structural differences in R

117 n in secondary structure predictions for the RNase P family.

118 ncode an RNA-based RNase P; activity of both RNase P forms from the same bacterium or archaeon could

119 ing (HTS) to identify specific inhibitors of RNase P from a 2880 compound library.

120 sfer RNA processing ribonucleoprotein enzyme RNase P from Escherichia coli.

121 specially once the structural differences in RNase P from the three domains of life have been establi

122 We also demonstrate that AACs interfere with RNase P function by displacing Mg2+ ions.

123 0) and MRPP3, each of which is essential for RNase P function.

124 t little is known about the role of HSD10 in RNase P function.

125 primers and a probe that targeted the human RNase P gene to assess the presence of PCR inhibitors an

126 fs of the hemotropic Mycoplasma 16S rRNA and RNase P genes indicate the presence of a novel organism.

127 Homologs of Aquifex RNase P (HARP) were identified in many Archaea and some

128 B. subtilis RNase P has a higher affinity for pre-tRNA with adenosin

129 few individual model substrates of bacterial RNase P have been well described, the competitive substr

130 irm that the protein- and RNA-based forms of RNase P have distinct modules for substrate recognition

131 y, where ribozymes, such as the ribosome and RNase P, have evolved into protein-dependent RNA catalys

132 onsensus and nonconsensus substrates for the RNase P holoenzyme are essentially uniform.

133 protein ensemble may be important for proper RNase P holoenzyme assembly and/or catalysis.

134 nsights suggest a possible role for I in the RNase P holoenzyme assembly process.

135 Although in bacteria the RNase P holoenzyme consists of one large catalytic RNA a

136 The protein component of the bacterial RNase P holoenzyme from Bacillus subtilis (P protein) wa

137 subunits, we have reconstituted in vitro the RNase P holoenzyme from the thermophilic archaeon Pyroco

138 crystal structure of the Thermotoga maritima RNase P holoenzyme in complex with tRNA(Phe).

139 A structure of the bacterial RNase P holoenzyme in complex with tRNAPhe revealed the

140 eal (an experimental surrogate for eukaryal) RNase P holoenzyme lends promise to the design of aminog

141 cture-function relationships of the archaeal RNase P holoenzyme.

142 the bacterial RNA component, and a bacterial RNase P holoenzyme/tRNA complex provide insights into th

143 fferent mesophilic and thermophilic archaeal RNase P holoenzymes, reconstituted in vitro using their

144 Arabidopsis thaliana, to employ protein-only RNase P in both its nucleus and organelles.

145 e identified an unknown type of protein-only RNase P in the hyperthermophilic bacterium Aquifex aeoli

146 ay beam to map the structure of 16S rRNA and RNase P in viable bacteria in situ.

147 ow that targeted destruction of HeLa nuclear RNase P inhibits transcription of 5S rRNA genes in whole

148 Nase MRP protein components, all shared with RNase P, interact with the substrate.

149 Archaeal RNase P is a ribonucleoprotein made up of one catalytic

150 Remarkably, in most organisms, RNase P is a ribonucleoprotein particle where the RNA co

151 RNase P is a ubiquitous and essential ribonucleoprotein

152 RNase P is a universal enzyme that removes 5' leader seq

153 nal behavior of cells harboring the chimeric RNAse P is also perturbed, affecting the levels of at le

154 Bacterial RNase P is an attractive potential antibacterial target

155 rovide evidence that the human mitochondrial RNase P is an entirely protein-based enzyme.

156 RNase P is an essential tRNA-processing enzyme in all do

157 RNase P is an RNA-based enzyme primarily responsible for

158 the endoribonucleolytic activity per se, of RNase P is critical for the function of Pol III in cells

159 ntify RNAs that do not change abundance when RNase P is depleted but accumulate as larger precursors,

160 The sequence preference of E. coli RNase P is diminished, showing a weak preference for ade

161 Eukaryotic nuclear RNase P is far more complex than in the bacterial form,

162 RNase P is formed by an RNA molecule responsible for cat

163 Human RNase P is implicated in transcription of small non-codi

164 The activity of the 4-thiouridine RNase P is partially rescued by addition of Cd(II) or Mn

165 RNase P is primarily responsible for the 5 maturation of

166 Here we report that RNase P is required for the initial separation of all se

167 Since bacterial RNase P is required for viability and differs in structu

168 RNase P is the enzyme that removes 5' leader sequences f

169 RNase P is the ubiquitous ribonucleoprotein metalloenzym

170 Among all enzymes in nature, RNase P is unique in that it can use either an RNA- or a

171 random EGSs, the particular target RNA, and RNase P is used in the diagnostic procedure, which, afte

172 Ribonuclease (RNase) P is a site-specific endoribonuclease found in al

173 Ribonuclease (RNase) P is the universal ribozyme responsible for 5'-en

174 Ribonuclease P (RNase P) is a Mg2+-dependent endoribonuclease responsibl

175 Ribonuclease P (RNase P) is a ribonucleoprotein (RNP) enzyme that cataly

176 Ribonuclease P (RNase P) is a ribonucleoprotein complex that utilizes a

177 Ribonuclease P (RNase P) is an endonuclease that catalyzes the essential

178 Ribonuclease P (RNase P) is an essential endonuclease responsible for th

179 Ribonuclease P (RNase P) is an essential endonuclease that catalyzes the

180 te nucleus, the endonuclease ribonuclease P (RNase P) is composed of a catalytic RNA that is assisted

181 Ribonuclease P (RNase P) is one of the first ribozymes discovered and it

182 The mitochondrial form of ribonuclease P (mt:RNase P) is responsible for 5'-end maturation and is com

183 In the eukaryotes, the RNase P lineage has split into two, giving rise to a clo

184 mechanism for cellular lncRNAs that display RNase P-mediated 3' end processing.

185 bstrate recognition while assisting archaeal RNase P-mediated cleavage of a target RNA in vitro.

186 The RNase P-mediated endonucleolytic cleavage plays a crucia

187 This in vivo mt:RNase P model will advance our understanding of how loss

188 orted here will further our understanding of RNase P molecular recognition and facilitate discovery o

189 e further evidence of a conserved eukaryotic RNase P/MRP architecture and provide a strong basis for

190 ents universally found in all enzymes of the RNase P/MRP family, as well as with a phylogenetically c

191 rganization of the eukaryotic enzymes of the RNase P/MRP family.

192 myces cerevisiae RNase MRP in a complex with RNase P/MRP proteins Pop6 and Pop7 solved to 2.7 A.

193 s with existing data for the yeast and human RNase P/MRP systems enables confident identification of

194 r to a protein-binding domain in the RNAs of RNase P/MRP.

195 ctural organization of the P3 RNA domains in RNases P/MRP and possible functions of the P3 domains an

196 structurally distinct RNPs, telomerase, and RNases P/MRP from unrelated progenitor RNAs.

197 The eukaryotic RNases P/MRP have acquired an essential helix-loop-helix

198 d the three proteins composing Drosophila mt:RNase P: Mulder (PRORP), Scully (MRPP2) and Roswell (MRP

199 the ribonucleoprotein enzyme ribonuclease P (RNase P (P RNA) contains the active site, but binding of

200 ularly significant is the mechanism by which RNase P processes the valU and lysT polycistronic transc

201 A single enzyme, ribonuclease P (RNase P), processes the 5' ends of tRNA precursors (ptRN

202 Based on the absolute requirement for RNase P processing of all three primary transcripts, ina

203 ndependent transcription terminator inhibits RNase P processing of both transcripts leading to a decr

204 uctural and biophysical studies of bacterial RNase P propose direct coordination of metal ions by the

205 However, protein-only RNase P (PRORP) enzymes process precursor tRNAs in human

206 larly, the recently discovered proteinaceous RNase P (PRORP) possesses two domains - pentatricopeptid

207 However, the discovery of protein-only RNase P (PRORP) shifted this paradigm, affording a uniqu

208 tter form of the enzyme, called protein-only RNase P (PRORP), is widespread in eukaryotes in which it

209 n (MRPP) 1 and 2 together with proteinaceous RNase P (PRORP).

210 Protein-only RNase Ps (PRORPs) are a recently discovered class of RNA

211 active site, but binding of Escherichia coli RNase P protein (C5) to P RNA increases the rate constan

212 s comprised of three proteins; mitochondrial RNase P protein (MRPP) 1 and 2 together with proteinaceo

213 5' side of the cleavage site (N(-4)) and the RNase P protein (P protein) subunit.

214 The bacterial RNase P protein (RPP) aids RNase P RNA (RPR) catalysis b

215 d of one catalytic RNase P RNA (RPR) and one RNase P protein (RPP), have helped understand the pleiot

216 tions in TRMT10C (encoding the mitochondrial RNase P protein 1 [MRPP1]) in two unrelated individuals

217 of pyrophosphate (PPi) to Bacillus subtilis RNase P protein as a model, we show that coupled reactio

218 est that an important biological function of RNase P protein is to offset differences in pre-tRNA str

219 However, the number of RNase P protein subunits (RPPs) varies from 1 in bacteri

220 ic RNase P RNA (RPR) and a varying number of RNase P proteins (RPPs): 1 in bacteria, at least 4 in ar

221 esent the most conserved region of bacterial RNase P proteins, exhibit negligible changes in catalyti

222 larly recruited suggesting that a variant of RNase P regulates H3.3 chromatin assembly.

223 RNase P represents a unique example of an enzyme that ca

224 ntriguing possibility is that replacement of RNase P ribonucleoprotein particles (RNPs) by proteins m

225 We constructed a functional RNase P ribozyme (M1GS RNA) that targets the overlapping

226 A functional RNase P ribozyme (M1GS RNA) was constructed to target th

227 lity of Salmonella-mediated oral delivery of RNase P ribozyme for gene-targeting applications in vivo

228 specificity domain of the Bacillus subtilis RNase P ribozyme undergoes a rate-limiting folding step

229 develop Salmonella-mediated gene transfer of RNase P ribozymes as an effective approach for gene-targ

230 n in animals and demonstrates the utility of RNase P ribozymes for gene targeting applications in viv

231 y, validate and analyze the genes coding for RNase P RNA (P RNA) from all published metagenomic proje

232 In particular, the precursor containing both RNase P RNA (RPM1) and tRNA(Pro) accumulated dramaticall

233 -maturation, typically comprises a catalytic RNase P RNA (RPR) and a varying number of RNase P protei

234 terial holoenzyme, composed of one catalytic RNase P RNA (RPR) and one RNase P protein (RPP), have he

235 The bacterial RNase P protein (RPP) aids RNase P RNA (RPR) catalysis by promoting substrate bindi

236 n all domains of life, it is a ribozyme: the RNase P RNA (RPR) component has been demonstrated to be

237 yrococcus furiosus (Pfu) L7Ae on its cognate RNase P RNA (RPR).

238 We identify in the Mma RNase P RNA a putative kink-turn (K-turn), the structura

239 nsights into the interaction between E. coli RNase P RNA and the -1 residue in the substrate.

240 ic and structural gap that separates the two RNase P RNA classes, previous work suggested their inter

241 both types of experiments indicate that the RNase P RNA folds similarly in 1 M Na(+) and 10 mM Mg(2+

242 energy landscape of the catalytic domain of RNase P RNA from Bacillus stearothermophilus (C(thermo))

243 The 260-residue catalytic domain of RNase P RNA from Bacillus stearothermophilus is immobili

244 Li and Altman computationally identified the RNase P RNA gene in all but three sequenced microbes: Na

245 identified a radically minimized form of the RNase P RNA in five Pyrobaculum species and the related

246 RNase P RNA is an ancient, nearly universal feature of l

247 y domain (S-domain) of the Bacillus subtilis RNase P RNA is more extended than its native structure.

248 roduct of the FAS II pathway is required for RNase P RNA maturation, which positively affects RNase P

249 were used to probe the binding sites on the RNase P RNA specificity domain of Bacillus subtilis.

250 e derived from RNA-RNA interactions with the RNase P RNA subunit.

251 of the B. subtilis and the Escherichia coli RNase P RNA that belong to different classes of P RNA an

252 The well-studied catalytic RNase P RNA uses a specificity module to recognize the p

253 acing the endogenous Type-A Escherichia coli RNase P RNA with a Type-B homolog derived from Bacillus

254 served noncoding RNAs from Escherichia coli, RNase P RNA, signal-recognition particle RNA, and tmRNA

255 , the -1 position, to study Escherichia coli RNase P RNA-mediated cleavage.

256 tly as yeast mitochondrial genomes encode an RNase P RNA.

257 aeal L7Ae in RNPs acting in tRNA processing (RNase P), RNA modification (H/ACA, C/D snoRNPs), and tra

258 e number and location of K-turns in archaeal RNase P RNAs (RPRs) are unclear.

259 The Pyrobaculum and Caldivirga RNase P RNAs are the smallest naturally occurring form y

260 In Bacteria, RNase P RNAs have been subdivided-based on their seconda

261 The "missing" RNase P RNAs in the other two species is perplexing give

262 ses that exist in eukaryotes: snRNA, snoRNA, RNase P, RNase MRP, Y RNA or telomerase RNA.

263 The protein component of yeast mitochondrial RNase P, Rpm2, is not modified by lipoic acid in the wil

264 Specifically, RNase P separates the tRNA units within each operon foll

265 y to follow the time-dependent folding of an RNase P specificity domain RNA.

266 esults support and extend current models for RNase P substrate recognition in which contacts involvin

267 Our data indicate that RNase P substrate recognition is more complex than previ

268 itive (TS) mutations in two of the essential RNase P subunits, Pop1p and Rpr1r.

269 9 modestly decrease the cleavage activity of RNase P, suggesting outer-sphere coordination of O6 on G

270 ence mirrors that observed for the RNA-based RNase P, suggesting similar catalytic mechanisms.

271 arable to their IC50 value for inhibition of RNase P, suggesting that binding of these antibiotics to

272 h RNase P and accumulate larger forms in the RNase P temperature-sensitive mutants.

273 RNA subunit of a ubiquitous endoribonuclease RNase P that consists of one RNA subunit and one or more

274 5), one of four protein subunits of archaeal RNase P that shares a homolog in the eukaryotic enzyme.

275 The universality of ribonuclease P (RNase P), the ribonucleoprotein essential for transfer R

276 highly conserved P4 helix of ribonuclease P (RNase P), the ribonucleoprotein that catalyzes the dival

277 ciding with the publication of a treatise on RNase P, this review provides a historical narrative, a

278 loss of the universal and supposedly ancient RNase P through genomic rearrangement at tRNA genes unde

279 d EGS variants that efficiently direct human RNase P to cleave a target mRNA in vitro.

280 mately 25-fold more active in inducing human RNase P to cleave the mRNA in vitro than the EGS derived

281 EGSs that are more robust in inducing human RNase P to cleave their targeted mRNAs.

282 The ability of RNase P to initiate tRNA processing at the 3' ends of lo

283 our kinetic and footprinting studies on Pfu RNase P, together with insights from recent structures o

284 t interactions critical for driving archaeal RNase P toward its functional conformation.

285 The active site structure and conserved RNase P-tRNA contacts suggest a universal mechanism of c

286 by Northern blot analysis with RNA from the RNase P TS mutants.

287 Our results suggest that protein-rich RNase P variants might have evolved to support flexibili

288 g preferentially with RNase MRP, rather than RNase P, via interactions with Snm1p and MRP RNA.

289 Second, RNase P was rapidly affinity-purified, and copurified RN

290 substrates compete for processing by E. coli RNase P, we compared the steady state reaction kinetics

291 ction studies and discovery of inhibitors of RNase P, we developed the first real-time RNase P activi

292 tent than neomycin B in inhibiting bacterial RNase P, we synthesized hexa-guanidinium and -lysyl conj

293 stand the assembly and catalysis of archaeal RNase P, we used a site-specific hydroxyl radical-mediat

294 of structure variation at sites contacted by RNase P, were determined by internal competition in reac

295 RNase P, which catalyzes the magnesium-dependent 5'-end

296 RNase P, which catalyzes tRNA 5'-maturation, typically c

297 ns that aid an RNA catalyst, we use archaeal RNase P, which comprises one catalytic RPR and at least

298 onuclease MRP is an endonuclease, related to RNase P, which functions in eukaryotic pre-rRNA processi

299 ise, Mg(2+)-dependent reconstitutions of Pfu RNase P with its catalytic RNA subunit and two interacti

300 ic activity but not for the formation of the RNase P x pre-tRNA (enzyme-substrate, ES) complex.