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  1 / 1251 MEDLINE  
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[PMID]:29059242
[Au] Autor:Sun X; Chen W; He L; Sheng J; Liu Y; Vu GP; Yang Z; Li W; Trang P; Wang Y; Hai R; Zhu H; Lu S; Liu F
[Ad] Endereço:College of Life Science and Technology, Jinan University, Guangzhou, Guangdong, China.
[Ti] Título:Inhibition of human cytomegalovirus immediate early gene expression and growth by a novel RNase P ribozyme variant.
[So] Source:PLoS One;12(10):e0186791, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We have previously engineered new RNase P-based ribozyme variants with improved in vitro catalytic activity. In this study, we employed a novel engineered variant to target a shared mRNA region of human cytomegalovirus (HCMV) immediate early proteins 1 (IE1) and 2 (IE2), which are essential for the expression of viral early and late genes as well as viral growth. Ribozyme F-R228-IE represents a novel variant that possesses three unique base substitution point mutations at the catalytic domain of RNase P catalytic RNA. Compared to F-M1-IE that is the ribozyme derived from the wild type RNase P catalytic RNA sequence, the functional variant F-R228-IE cleaved the target mRNA sequence in vitro at least 100 times more efficiently. In cultured cells, expression of F-R228-IE resulted in IE1/IE2 expression reduction by 98-99% and in HCMV production reduction by 50,000 folds. In contrast, expression of F-M1-IE resulted in IE1/IE2 expression reduction by less than 80% and in viral production reduction by 200 folds. Studies of the ribozyme-mediated antiviral effects in cultured cells suggest that overall viral early and late gene expression and viral growth were inhibited due to the ribozyme-mediated reduction of HCMV IE1 and IE2 expression. Our results provide direct evidence that engineered RNase P ribozymes, such as F-R228-IE, can serve as a novel class of inhibitors for the treatment and prevention of HCMV infection. Moreover, these results suggest that F-R228-IE, with novel and unique mutations at the catalytic domain to enhance ribozyme activity, can be a candidate for the construction of effective agents for anti-HCMV therapy.
[Mh] Termos MeSH primário: Citomegalovirus/genética
Genes Precoces
RNA Catalítico/metabolismo
Ribonuclease P/metabolismo
[Mh] Termos MeSH secundário: Citomegalovirus/crescimento & desenvolvimento
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Catalytic); EC 3.1.26.5 (Ribonuclease P)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171024
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186791


  2 / 1251 MEDLINE  
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[PMID]:28935369
[Au] Autor:Gao X; Oshima K; Ueda T; Nakashima T; Kimura M
[Ad] Endereço:Laboratory of Structural Biology, Graduate School of Systems Life Sciences, Hakozaki 6-10-1, Fukuoka, 812-8581, Japan.
[Ti] Título:A three-dimensional model of RNase P in the hyperthermophilic archaeon Pyrococcus horikoshii OT3.
[So] Source:Biochem Biophys Res Commun;493(2):1063-1068, 2017 Nov 18.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ribonuclease P (RNase P) is an endoribonuclease involved in maturation of the 5'-end of tRNA. We found previously that RNase P in the hyperthermophilic archaeon Pyrococcus horikoshii OT3 consists of a catalytic RNase P RNA (PhopRNA) and five protein cofactors designated PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38. The crystal structures of the five proteins have been determined, a three-dimensional (3-D) model of PhopRNA has been constructed, and biochemical data, including protein-RNA interaction sites, have become available. Here, this information was combined to orient the crystallographic structures of the proteins relative to their RNA binding sites in the PhopRNA model. Some alterations were made to the PhopRNA model to improve the fit. In the resulting structure, a heterotetramer composed of PhoPop5 and PhoRpp30 bridges helices P3 and P16 in the PhopRNA C-domain, thereby probably stabilizing a double-stranded RNA structure (helix P4) containing catalytic Mg ions, while a heterodimer of PhoRpp21 and PhoRpp29 locates on a single-stranded loop connecting helices P11 and P12 in the specificity domain (S-domain) in PhopRNA, probably forming an appropriate conformation of the precursor tRNA (pre-tRNA) binding site. The fifth protein PhoRpp38 binds each kink-turn (K-turn) motif in helices P12.1, P12.2, and P16 in PhopRNA. Comparison of the structure of the resulting 3-D model with that of bacterial RNase P suggests transition from RNA-RNA interactions in bacterial RNase P to protein-RNA interactions in archaeal RNase P. The proposed 3-D model of P. horikoshii RNase P will serve as a framework for further structural and functional studies on archaeal, as well as eukaryotic, RNase Ps.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Pyrococcus horikoshii/química
RNA Arqueal/química
Ribonuclease P/química
[Mh] Termos MeSH secundário: Sítios de Ligação
Cristalografia por Raios X
Modelos Moleculares
Conformação de Ácido Nucleico
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (RNA, Archaeal); EC 3.1.26.5 (Ribonuclease P)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170923
[St] Status:MEDLINE


  3 / 1251 MEDLINE  
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[PMID]:28934475
[Au] Autor:Incarnato D; Morandi E; Anselmi F; Simon LM; Basile G; Oliviero S
[Ad] Endereço:Dipartimento di Scienze della Vita e Biologia dei Sistemi, Università di Torino, Via Accademia Albertina, 13, Torino, Italy.
[Ti] Título:In vivo probing of nascent RNA structures reveals principles of cotranscriptional folding.
[So] Source:Nucleic Acids Res;45(16):9716-9725, 2017 Sep 19.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Defining the in vivo folding pathway of cellular RNAs is essential to understand how they reach their final native conformation. We here introduce a novel method, named Structural Probing of Elongating Transcripts (SPET-seq), that permits single-base resolution analysis of transcription intermediates' secondary structures on a transcriptome-wide scale, enabling base-resolution analysis of the RNA folding events. Our results suggest that cotranscriptional RNA folding in vivo is a mixture of cooperative folding events, in which local RNA secondary structure elements are formed as they get transcribed, and non-cooperative events, in which 5'-halves of long-range helices get sequestered into transient non-native interactions until their 3' counterparts have been transcribed. Together our work provides the first transcriptome-scale overview of RNA cotranscriptional folding in a living organism.
[Mh] Termos MeSH primário: Dobramento de RNA
RNA/química
[Mh] Termos MeSH secundário: Bioquímica/métodos
Escherichia coli/genética
Conformação de Ácido Nucleico
Ribonuclease P/química
Ribonuclease P/metabolismo
Ésteres do Ácido Sulfúrico/química
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Sulfuric Acid Esters); 63231-63-0 (RNA); EC 3.1.26.5 (Ribonuclease P); JW5CW40Z50 (dimethyl sulfate)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170922
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx617


  4 / 1251 MEDLINE  
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[PMID]:28808133
[Au] Autor:Bowden KE; Wiese NS; Perwez T; Mohanty BK; Kushner SR
[Ad] Endereço:Department of Genetics, University of Georgia, Athens, Georgia, USA.
[Ti] Título:The -Encoded Truncated RNase PH Protein Inhibits RNase P Maturation of Pre-tRNAs with Short Leader Sequences in the Absence of RppH.
[So] Source:J Bacteriol;199(22), 2017 Nov 15.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RNase PH, encoded by the gene, is a 3'→5' exoribonuclease that in participates primarily in the 3' maturation of pre-tRNAs and the degradation of rRNA in stationary-phase cells. Interestingly, the routinely used laboratory strains of MG1655 and W3110 have naturally acquired the allele, encoding a truncated catalytically inactive RNase PH protein which is widely assumed to be benign. Contrary to this assumption, we show that the -encoded Rph-1 protein inhibits RNase P-mediated 5'-end maturation of primary pre-tRNAs with leaders of <5 nucleotides in the absence of RppH, an RNA pyrophosphohydrolase. In contrast, RppH is not required for 5'-end maturation of endonucleolytically generated pre-tRNAs in the strain and for any tRNAs in Δ mutant or strains. We propose that the Rph-1 protein bound to the 3' end of the substrate creates a steric hindrance that in the presence of a triphosphate at the 5' end reduces the ability of RNase P to bind to the pre-tRNA. In this paper, we demonstrate that the mutation found in commonly used strains leads to the synthesis of a truncated functionally inactive RNase PH protein that interferes with the 5'-end maturation of specific tRNAs with short 5' leaders by RNase P in the absence of RppH, an RNA pyrophosphohydrolase that converts primary 5' triphosphates into 5' monophosphates. The data presented indicate that the presence of the triphosphate interferes with RNase P binding to the pre-tRNA.
[Mh] Termos MeSH primário: Hidrolases Anidrido Ácido/genética
Hidrolases Anidrido Ácido/metabolismo
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Exorribonucleases/genética
RNA de Transferência/metabolismo
Ribonuclease P/metabolismo
[Mh] Termos MeSH secundário: Endorribonucleases/genética
Endorribonucleases/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Exorribonucleases/metabolismo
Mutação
Sinais Direcionadores de Proteínas
Precursores de RNA/química
Precursores de RNA/genética
Precursores de RNA/metabolismo
Processamento Pós-Transcricional do RNA
RNA Bacteriano/genética
RNA Bacteriano/metabolismo
RNA de Transferência/química
RNA de Transferência/genética
Ribonuclease P/genética
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Protein Sorting Signals); 0 (RNA Precursors); 0 (RNA, Bacterial); 9014-25-9 (RNA, Transfer); EC 2.7.7.56 (ribonuclease PH); EC 3.1.- (Endoribonucleases); EC 3.1.- (Exoribonucleases); EC 3.1.26.5 (Ribonuclease P); EC 3.1.4.- (ribonuclease E); EC 3.6.- (Acid Anhydride Hydrolases); EC 3.6.1.- (RppH protein, E coli)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170816
[St] Status:MEDLINE


  5 / 1251 MEDLINE  
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[PMID]:28715256
[Au] Autor:Kimura M
[Ad] Endereço:a Laboratory of Biochemistry, Department of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School , Kyushu University , Fukuoka , Japan.
[Ti] Título:Structural basis for activation of an archaeal ribonuclease P RNA by protein cofactors.
[So] Source:Biosci Biotechnol Biochem;81(9):1670-1680, 2017 Sep.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ribonuclease P (RNase P) is an endoribonuclease that catalyzes the processing of the 5'-leader sequence of precursor tRNA (pre-tRNA) in all phylogenetic domains. We have found that RNase P in the hyperthermophilic archaeon Pyrococcus horikoshii OT3 consists of RNase P RNA (PhopRNA) and five protein cofactors designated PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38. Biochemical characterizations over the past 10 years have revealed that PhoPop5 and PhoRpp30 fold into a heterotetramer and cooperate to activate a catalytic domain (C-domain) in PhopRNA, whereas PhoRpp21 and PhoRpp29 form a heterodimer and function together to activate a specificity domain (S-domain) in PhopRNA. PhoRpp38 plays a role in elevation of the optimum temperature of RNase P activity, binding to kink-turn (K-turn) motifs in two stem-loops in PhopRNA. This review describes the structural and functional information on P. horikoshii RNase P, focusing on the structural basis for the PhopRNA activation by the five RNase P proteins.
[Mh] Termos MeSH primário: Proteínas Arqueais/metabolismo
Pyrococcus horikoshii/genética
Pyrococcus horikoshii/metabolismo
RNA Arqueal/metabolismo
RNA de Transferência/metabolismo
Ribonuclease P/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Seres Humanos
RNA Arqueal/genética
Ribonuclease P/química
Ribonuclease P/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (RNA, Archaeal); 9014-25-9 (RNA, Transfer); EC 3.1.26.5 (Ribonuclease P)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170718
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2017.1353404


  6 / 1251 MEDLINE  
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[PMID]:28696260
[Au] Autor:Pinker F; Schelcher C; Fernandez-Millan P; Gobert A; Birck C; Thureau A; Roblin P; Giegé P; Sauter C
[Ad] Endereço:From the Université de Strasbourg, CNRS, Institut de Biologie Moléculaire et Cellulaire, Architecture et Réactivité de l'ARN, UPR 9002, F-67000 Strasbourg, France.
[Ti] Título:Biophysical analysis of protein-only RNase P alone and in complex with tRNA provides a refined model of tRNA binding.
[So] Source:J Biol Chem;292(34):13904-13913, 2017 Aug 25.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RNase P is a universal enzyme that removes 5' leader sequences from tRNA precursors. The enzyme is therefore essential for maturation of functional tRNAs and mRNA translation. RNase P represents a unique example of an enzyme that can occur either as ribonucleoprotein or as protein alone. The latter form of the enzyme, called protein-only RNase P (PRORP), is widespread in eukaryotes in which it can provide organellar or nuclear RNase P activities. Here, we have focused on nuclear PRORP2 and its interaction with tRNA substrates. Affinity measurements helped assess the respective importance of individual pentatricopeptide repeat motifs in PRORP2 for RNA binding. We characterized the PRORP2 structure by X-ray crystallography and by small-angle X-ray scattering in solution as well as that of its complex with a tRNA precursor by small-angle X-ray scattering. Of note, our study reports the first structural data of a PRORP-tRNA complex. Combined with complementary biochemical and biophysical analyses, our structural data suggest that PRORP2 undergoes conformational changes to accommodate its substrate. In particular, the catalytic domain and the RNA-binding domain can move around a central hinge. Altogether, this work provides a refined model of the PRORP-tRNA complex that illustrates how protein-only RNase P enzymes specifically bind tRNA and highlights the contribution of protein dynamics to achieve this specific interaction.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/metabolismo
Modelos Moleculares
Precursores de RNA/metabolismo
Processamento Pós-Transcricional do RNA
RNA de Plantas/metabolismo
RNA de Transferência de Cisteína/metabolismo
Ribonuclease P/metabolismo
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Substituição de Aminoácidos
Arabidopsis/enzimologia
Proteínas de Arabidopsis/química
Proteínas de Arabidopsis/genética
Fenômenos Biofísicos
Domínio Catalítico
Estabilidade Enzimática
Mutação
Conformação de Ácido Nucleico
Motivos de Nucleotídeos
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
RNA/química
RNA/metabolismo
Precursores de RNA/química
RNA de Plantas/química
RNA de Transferência de Cisteína/química
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Ribonuclease P/química
Ribonuclease P/genética
Solubilidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Peptide Fragments); 0 (RNA Precursors); 0 (RNA, Plant); 0 (RNA, Transfer, Cys); 0 (RNA, recombinant); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 63231-63-0 (RNA); EC 3.1.26.5 (PRORP2 protein, Arabidopsis); EC 3.1.26.5 (Ribonuclease P)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170712
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.782078


  7 / 1251 MEDLINE  
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[PMID]:28694328
[Au] Autor:Niland CN; Anderson DR; Jankowsky E; Harris ME
[Ad] Endereço:Department of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106, USA.
[Ti] Título:The contribution of the C5 protein subunit of ribonuclease P to specificity for precursor tRNA is modulated by proximal 5' leader sequences.
[So] Source:RNA;23(10):1502-1511, 2017 Oct.
[Is] ISSN:1469-9001
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recognition of RNA by RNA processing enzymes and RNA binding proteins often involves cooperation between multiple subunits. However, the interdependent contributions of RNA and protein subunits to molecular recognition by ribonucleoproteins are relatively unexplored. RNase P is an endonuclease that removes 5' leaders from precursor tRNAs and functions in bacteria as a dimer formed by a catalytic RNA subunit (P RNA) and a protein subunit (C5 in ). The P RNA subunit contacts the tRNA body and proximal 5' leader sequences [N(-1) and N(-2)] while C5 binds distal 5' leader sequences [N(-3) to N(-6)]. To determine whether the contacts formed by P RNA and C5 contribute independently to specificity or exhibit cooperativity or anti-cooperativity, we compared the relative / values for all possible combinations of the six proximal 5' leader nucleotides ( = 4096) for processing by the P RNA subunit alone and by the RNase P holoenzyme. We observed that while the P RNA subunit shows specificity for 5' leader nucleotides N(-2) and N(-1), the presence of the C5 protein reduces the contribution of P RNA to specificity, but changes specificity at N(-2) and N(-3). The results reveal that the contribution of C5 protein to RNase P processing is controlled by the identity of N(-2) in the pre-tRNA 5' leader. The data also clearly show that pairing of the 5' leader with the 3' ACCA of tRNA acts as an anti-determinant for RNase P cleavage. Comparative analysis of genomically encoded tRNAs reveals that both anti-determinants are subject to negative selection in vivo.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/metabolismo
Precursores de RNA/metabolismo
RNA de Transferência/metabolismo
Ribonuclease P/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Escherichia coli/química
Nucleotídeos/química
Nucleotídeos/metabolismo
Precursores de RNA/química
RNA de Transferência/química
RNA de Transferência de Metionina/química
RNA de Transferência de Metionina/metabolismo
Ribonuclease P/química
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Nucleotides); 0 (RNA Precursors); 0 (RNA, Transfer, Met); 9014-25-9 (RNA, Transfer); EC 3.1.26.5 (Ribonuclease P); EC 3.1.26.5 (ribonuclease P, E coli)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170712
[St] Status:MEDLINE
[do] DOI:10.1261/rna.056408.116


  8 / 1251 MEDLINE  
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[PMID]:28597298
[Au] Autor:Hausrath AC; Kingston RL
[Ad] Endereço:School of Biological Sciences, The University of Auckland, Auckland, 1010, New Zealand.
[Ti] Título:Conditionally disordered proteins: bringing the environment back into the fold.
[So] Source:Cell Mol Life Sci;74(17):3149-3162, 2017 Sep.
[Is] ISSN:1420-9071
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:For many proteins, biological function requires the folding of the polypeptide chain into a unique and persistent tertiary structure. This review concerns proteins that adopt a specific tertiary structure to function, but are otherwise partially or completely disordered. The biological cue for protein folding is environmental perturbation or minor post-translational modification. Hence, we term these proteins conditionally disordered. Many of these proteins recognize and bind other molecules, and conditional disorder has been hypothesized to allow for more nuanced control and regulation of binding processes. However, this remains largely unproven. The sequences of conditionally disordered proteins suggest their propensity to fold; yet, under the standard laboratory conditions, they do not do so, which may appear surprising. We argue that the surprise results from the failure to consider the role of the environment in protein structure formation and that conditional disorder arises as a natural consequence of the marginal stability of the folded state.
[Mh] Termos MeSH primário: Proteínas Intrinsicamente Desordenadas/metabolismo
[Mh] Termos MeSH secundário: Bactérias/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Fator de Iniciação 4E em Eucariotos/química
Fator de Iniciação 4E em Eucariotos/metabolismo
Proteínas HMGB/química
Proteínas HMGB/metabolismo
Seres Humanos
Proteínas Intrinsicamente Desordenadas/química
Ligação Proteica
Dobramento de Proteína
Estrutura Terciária de Proteína
Receptores de Glucocorticoides/química
Receptores de Glucocorticoides/metabolismo
Ribonuclease P/química
Ribonuclease P/metabolismo
Fatores de Transcrição/química
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Eukaryotic Initiation Factor-4E); 0 (HMGB Proteins); 0 (Intrinsically Disordered Proteins); 0 (Receptors, Glucocorticoid); 0 (Transcription Factors); EC 3.1.26.5 (Ribonuclease P)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170830
[Lr] Data última revisão:
170830
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170610
[St] Status:MEDLINE
[do] DOI:10.1007/s00018-017-2558-1


  9 / 1251 MEDLINE  
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[PMID]:28525600
[Au] Autor:Lai LB; Tanimoto A; Lai SM; Chen WY; Marathe IA; Westhof E; Wysocki VH; Gopalan V
[Ad] Endereço:Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.
[Ti] Título:A novel double kink-turn module in euryarchaeal RNase P RNAs.
[So] Source:Nucleic Acids Res;45(12):7432-7440, 2017 Jul 07.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:RNase P is primarily responsible for the 5΄ maturation of transfer RNAs (tRNAs) in all domains of life. Archaeal RNase P is a ribonucleoprotein made up of one catalytic RNA and five protein cofactors including L7Ae, which is known to bind the kink-turn (K-turn), an RNA structural element that causes axial bending. However, the number and location of K-turns in archaeal RNase P RNAs (RPRs) are unclear. As part of an integrated approach, we used native mass spectrometry to assess the number of L7Ae copies that bound the RPR and site-specific hydroxyl radical-mediated footprinting to localize the K-turns. Mutagenesis of each of the putative K-turns singly or in combination decreased the number of bound L7Ae copies, and either eliminated or changed the L7Ae footprint on the mutant RPRs. In addition, our results support an unprecedented 'double K-turn' module in type A and type M archaeal RPR variants.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Regulação da Expressão Gênica em Archaea
Methanocaldococcus/enzimologia
Pyrococcus furiosus/enzimologia
RNA Arqueal/química
RNA de Transferência/química
Ribonuclease P/química
[Mh] Termos MeSH secundário: Proteínas Arqueais/genética
Proteínas Arqueais/metabolismo
Sequência de Bases
Radical Hidroxila/química
Radical Hidroxila/metabolismo
Isoenzimas/química
Isoenzimas/genética
Isoenzimas/metabolismo
Methanocaldococcus/genética
Mathanococcus/enzimologia
Mathanococcus/genética
Mutação
Conformação de Ácido Nucleico
Ligação Proteica
Pyrococcus furiosus/genética
Precursores de RNA
RNA Arqueal/genética
RNA Arqueal/metabolismo
RNA de Transferência/genética
RNA de Transferência/metabolismo
Ribonuclease P/genética
Ribonuclease P/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Isoenzymes); 0 (RNA Precursors); 0 (RNA, Archaeal); 3352-57-6 (Hydroxyl Radical); 9014-25-9 (RNA, Transfer); EC 3.1.26.5 (Ribonuclease P)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170520
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx388


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[PMID]:28499021
[Au] Autor:Gößringer M; Lechner M; Brillante N; Weber C; Rossmanith W; Hartmann RK
[Ad] Endereço:Institute of Pharmaceutical Chemistry, Philipps-University Marburg, Marbacher Weg 6, 35037 Marburg, Germany.
[Ti] Título:Protein-only RNase P function in Escherichia coli: viability, processing defects and differences between PRORP isoenzymes.
[So] Source:Nucleic Acids Res;45(12):7441-7454, 2017 Jul 07.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The RNase P family comprises structurally diverse endoribonucleases ranging from complex ribonucleoproteins to single polypeptides. We show that the organellar (AtPRORP1) and the two nuclear (AtPRORP2,3) single-polypeptide RNase P isoenzymes from Arabidopsis thaliana confer viability to Escherichia coli cells with a lethal knockdown of its endogenous RNA-based RNase P. RNA-Seq revealed that AtPRORP1, compared with bacterial RNase P or AtPRORP3, cleaves several precursor tRNAs (pre-tRNAs) aberrantly in E. coli. Aberrant cleavage by AtPRORP1 was mainly observed for pre-tRNAs that can form short acceptor-stem extensions involving G:C base pairs, including tRNAAsp(GUC), tRNASer(CGA) and tRNAHis. However, both AtPRORP1 and 3 were defective in processing of E. coli pre-tRNASec carrying an acceptor stem expanded by three G:C base pairs. Instead, pre-tRNASec was degraded, suggesting that tRNASec is dispensable for E. coli under laboratory conditions. AtPRORP1, 2 and 3 are also essentially unable to process the primary transcript of 4.5S RNA, a hairpin-like non-tRNA substrate processed by E. coli RNase P, indicating that PRORP enzymes have a narrower, more tRNA-centric substrate spectrum than bacterial RNA-based RNase P enzymes. The cells' viability also suggests that the essential function of the signal recognition particle can be maintained with a 5΄-extended 4.5S RNA.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/genética
Escherichia coli/genética
Regulação Bacteriana da Expressão Gênica
Precursores de RNA/genética
Ribonuclease P/genética
[Mh] Termos MeSH secundário: Arabidopsis/genética
Arabidopsis/metabolismo
Proteínas de Arabidopsis/genética
Proteínas de Arabidopsis/metabolismo
Pareamento de Bases
Sequência de Bases
Escherichia coli/metabolismo
Proteínas de Escherichia coli/metabolismo
Teste de Complementação Genética
Viabilidade Microbiana
Conformação de Ácido Nucleico
Precursores de RNA/metabolismo
RNA Bacteriano/genética
RNA Bacteriano/metabolismo
RNA de Transferência de Ácido Aspártico/genética
RNA de Transferência de Ácido Aspártico/metabolismo
RNA de Transferência de Histidina/genética
RNA de Transferência de Histidina/metabolismo
RNA de Transferência de Serina/genética
RNA de Transferência de Serina/metabolismo
Ribonuclease P/deficiência
Ribonuclease P/metabolismo
Transgenes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (4.5S RNA); 0 (Arabidopsis Proteins); 0 (Escherichia coli Proteins); 0 (RNA Precursors); 0 (RNA, Bacterial); 0 (RNA, Transfer, Asp); 0 (RNA, Transfer, His); 0 (RNA, Transfer, Ser); EC 3.1.26.5 (PRORP1 protein, Arabidopsis); EC 3.1.26.5 (PRORP2 protein, Arabidopsis); EC 3.1.26.5 (PRORP3 protein, Arabidopsis); EC 3.1.26.5 (Ribonuclease P)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170513
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx405



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