Binding of C5 protein to P RNA enhances the rate constant for catalysis for P RNA processing of pre-tRNAs lacking a consensus (+ 1)/C(+ 72) pair (Q36136464)

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English	Binding of C5 protein to P RNA enhances the rate constant for catalysis for P RNA processing of pre-tRNAs lacking a consensus (+ 1)/C(+ 72) pair	scientific article

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

Binding of C5 protein to P RNA enhances the rate constant for catalysis for P RNA processing of pre-tRNAs lacking a consensus (+ 1)/C(+ 72) pair (English)

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

author name string

Lei Sun

1

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Europe PubMed Central

PMC publication ID

12 August 2017

Frank E Campbell

2

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Europe PubMed Central

PMC publication ID

12 August 2017

Lindsay E Yandek

3

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Europe PubMed Central

PMC publication ID

12 August 2017

Michael E Harris

4

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Europe PubMed Central

PMC publication ID

12 August 2017

language of work or name

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publication date

13 November 2009

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Europe PubMed Central

PMC publication ID

12 August 2017

Journal of Molecular Biology

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Europe PubMed Central

PMC publication ID

12 August 2017

395

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Europe PubMed Central

PMC publication ID

12 August 2017

5

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Europe PubMed Central

PMC publication ID

12 August 2017

1019-1037

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

describes a project that uses

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Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC3410724/fullTextXML

based on heuristic

inferred from PubMed Central ID database lookup

Different aa-tRNAs are selected uniformly on the ribosome

1 reference

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2 October 2017

Importance of RNA-protein interactions in bacterial ribonuclease P structure and catalysis

1 reference

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2 October 2017

Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinity

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 October 2017

RNase P RNA mediated cleavage: substrate recognition and catalysis

1 reference

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2 October 2017

Probing the architecture of the B. subtilis RNase P holoenzyme active site by cross-linking and affinity cleavage

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 October 2017

Alternative roles for metal ions in enzyme catalysis and the implications for ribozyme chemistry

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 October 2017

The precursor tRNA 3'-CCA interaction with Escherichia coli RNase P RNA is essential for catalysis by RNase P in vivo

1 reference

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2 October 2017

Bacterial RNase P: a new view of an ancient enzyme

1 reference

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2 October 2017

RNase P: interface of the RNA and protein worlds

1 reference

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2 October 2017

Type A and B RNase P RNAs are interchangeable in vivo despite substantial biophysical differences.

1 reference

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2 October 2017

The naturally trans-acting ribozyme RNase P RNA has leadzyme properties

1 reference

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2 October 2017

Protein activation of a ribozyme: the role of bacterial RNase P protein

1 reference

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2 October 2017

Substrate discrimination in RNase P RNA-mediated cleavage: importance of the structural environment of the RNase P cleavage site

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 October 2017

Compilation of tRNA sequences and sequences of tRNA genes

1 reference

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2 October 2017

The spliceosome: the most complex macromolecular machine in the cell?

1 reference

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2 October 2017

Recognition of the 5' leader of pre-tRNA substrates by the active site of ribonuclease P.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 October 2017

Evidence for a polynuclear metal ion binding site in the catalytic domain of ribonuclease P RNA.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 October 2017

Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 October 2017

Helix P4 is a divalent metal ion binding site in the conserved core of the ribonuclease P ribozyme

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 October 2017

Protein component of the ribozyme ribonuclease P alters substrate recognition by directly contacting precursor tRNA

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 October 2017

RNase P from bacteria. Substrate recognition and function of the protein subunit

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 October 2017

Ribonuclease P (RNase P) RNA is converted to a Cd(2+)-ribozyme by a single Rp-phosphorothioate modification in the precursor tRNA at the RNase P cleavage site

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 October 2017

Determinants of Escherichia coli RNase P cleavage site selection: a detailed in vitro and in vivo analysis.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 October 2017

Base pairing between Escherichia coli RNase P RNA and its substrate

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 October 2017

Interaction of the 3′-end of tRNA with ribonuclease P RNA

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 October 2017

Mapping the active site of ribonuclease P RNA using a substrate containing a photoaffinity agent.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 October 2017

The kinetics and specificity of cleavage by RNase P is mainly dependent on the structure of the amino acid acceptor stem

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 October 2017

In vivo and in vitro investigation of bacterial type B RNase P interaction with tRNA 3'-CCA.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 July 2018

Evidence that substrate-specific effects of C5 protein lead to uniformity in binding and catalysis by RNase P.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 July 2018

Recognition of the 5' leader and the acceptor stem of a pre-tRNA substrate by the ribozyme from Bacillus subtilis RNase P.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 July 2018

Kinetics and thermodynamics of the RNase P RNA cleavage reaction: analysis of tRNA 3'-end variants.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 July 2018

Influence of metal ions on the ribonuclease P reaction. Distinguishing substrate binding from catalysis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

2 July 2018

A 2'-methyl or 2'-methylene group at G+1 in precursor tRNA interferes with Mg2+ binding at the enzyme-substrate interface in E-S complexes of E. coli RNase P.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

23 September 2018

The P4 metal binding site in RNase P RNA affects active site metal affinity through substrate positioning

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

23 September 2018

RNA-dependent folding and stabilization of C5 protein during assembly of the E. coli RNase P holoenzyme.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

23 September 2018

The exocyclic amine at the RNase P cleavage site contributes to substrate binding and catalysis.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

23 September 2018

The 5' leader of precursor tRNAAsp bound to the Bacillus subtilis RNase P holoenzyme has an extended conformation.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

23 September 2018

Complexity in orchestration of chemical groups near different cleavage sites in RNase P RNA mediated cleavage

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

23 September 2018

The pre-tRNA nucleotide base and 2'-hydroxyl at N(-1) contribute to fidelity in tRNA processing by RNase P.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

23 September 2018

The residue immediately upstream of the RNase P cleavage site is a positive determinant

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

23 September 2018

Conservation of helical structure contributes to functional metal ion interactions in the catalytic domain of ribonuclease P RNA.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

23 September 2018

Exploring the minimal substrate requirements for trans-cleavage by RNase P holoenzymes from Escherichia coli and Bacillus subtilis.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

23 September 2018

Evidence for helical unwinding of an RNA substrate by the RNA enzyme RNase P: use of an interstrand disulfide crosslink in substrate.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

23 September 2018

Maturation of pre-tRNA(fMet) by Escherichia coli RNase P is specified by a guanosine of the 5'-flanking sequence.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3410724

23 September 2018

A kinetic mechanism for cleavage of precursor tRNA(Asp) catalyzed by the RNA component of Bacillus subtilis ribonuclease P

1 reference

https://pubmed.ncbi.nlm.nih.gov/19917291

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Building a kinetic framework for group II intron ribozyme activity: quantitation of interdomain binding and reaction rate

1 reference

https://pubmed.ncbi.nlm.nih.gov/19917291

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Protein component of Bacillus subtilis RNase P specifically enhances the affinity for precursor-tRNAAsp

1 reference

https://pubmed.ncbi.nlm.nih.gov/19917291

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Role of base G-2 of pre-tRNAfMet in cleavage site selection by Escherichia coli RNase P in vitro

1 reference

https://pubmed.ncbi.nlm.nih.gov/19917291

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based on heuristic

inferred from PubMed ID database lookup

Recognition of a pre-tRNA substrate by the Bacillus subtilis RNase P holoenzyme

1 reference

https://pubmed.ncbi.nlm.nih.gov/19917291

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identification of individual nucleotides in the bacterial ribonuclease P ribozyme adjacent to the pre-tRNA cleavage site by short-range photo-cross-linking

1 reference

https://pubmed.ncbi.nlm.nih.gov/19917291

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identification of adenosine functional groups involved in substrate binding by the ribonuclease P ribozyme

1 reference

https://pubmed.ncbi.nlm.nih.gov/19917291

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The cleavage step of ribonuclease P catalysis is determined by ribozyme-substrate interactions both distal and proximal to the cleavage site

1 reference

https://pubmed.ncbi.nlm.nih.gov/19917291

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based on heuristic

inferred from PubMed ID database lookup

Idiosyncratic tuning of tRNAs to achieve uniform ribosome binding

1 reference

https://pubmed.ncbi.nlm.nih.gov/19917291

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Structural perspective on the activation of RNase P RNA by protein

1 reference

https://pubmed.ncbi.nlm.nih.gov/19917291

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The affinity of magnesium binding sites in the Bacillus subtilis RNase P x pre-tRNA complex is enhanced by the protein subunit

1 reference

https://pubmed.ncbi.nlm.nih.gov/19917291

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Importance of the +73/294 interaction in Escherichia coli RNase P RNA substrate complexes for cleavage and metal ion coordination

1 reference

https://pubmed.ncbi.nlm.nih.gov/19917291

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based on heuristic

inferred from PubMed ID database lookup

Ion dependence of the Bacillus subtilis RNase P reaction

1 reference

https://pubmed.ncbi.nlm.nih.gov/19917291

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1016/J.JMB.2009.11.027

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

ResearchGate publication ID

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