RnpA

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  • Description: protein component of RNase P, metal-dependent 5' end maturation of precursor tRNAs

Gene name rnpA
Synonyms
Essential yes PubMed
Product protein component of RNase P (substrate specificity)
Function cleavage of precursor sequences
from the 5' ends of pre-tRNAs
Gene expression levels in SubtiExpress: rnpA
Interactions involving this protein in SubtInteract: RnpA
MW, pI 13 kDa, 10.804
Gene length, protein length 348 bp, 116 aa
Immediate neighbours spoIIIJ, rpmH
Sequences Protein DNA DNA_with_flanks
Genetic context
ThdF jag spoIIIJ rnpA rpmH context.png
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RnpA expression.png
















Categories containing this gene/protein

Rnases, translation, essential genes

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU41050

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor (according to Swiss-Prot)
  • Protein family: rnpA family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
    • expression transiently increases in the forespore PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Roland K Hartmann, Markus Gössringer, Bettina Späth, Susan Fischer, Anita Marchfelder
The making of tRNAs and more - RNase P and tRNase Z.
Prog Mol Biol Transl Sci: 2009, 85;319-68
[PubMed:19215776] [WorldCat.org] [DOI] (P p)

J Kristin Smith, John Hsieh, Carol A Fierke
Importance of RNA-protein interactions in bacterial ribonuclease P structure and catalysis.
Biopolymers: 2007, 87(5-6);329-38
[PubMed:17868095] [WorldCat.org] [DOI] (P p)

Alexei V Kazantsev, Norman R Pace
Bacterial RNase P: a new view of an ancient enzyme.
Nat Rev Microbiol: 2006, 4(10);729-40
[PubMed:16980936] [WorldCat.org] [DOI] (I p)

Donald Evans, Steven M Marquez, Norman R Pace
RNase P: interface of the RNA and protein worlds.
Trends Biochem Sci: 2006, 31(6);333-41
[PubMed:16679018] [WorldCat.org] [DOI] (P p)

Alfredo Torres-Larios, Kerren K Swinger, Tao Pan, Alfonso Mondragón
Structure of ribonuclease P--a universal ribozyme.
Curr Opin Struct Biol: 2006, 16(3);327-35
[PubMed:16650980] [WorldCat.org] [DOI] (P p)

John Hsieh, Andy J Andrews, Carol A Fierke
Roles of protein subunits in RNA-protein complexes: lessons from ribonuclease P.
Biopolymers: 2004, 73(1);79-89
[PubMed:14691942] [WorldCat.org] [DOI] (P p)

Enno Hartmann, Roland K Hartmann
The enigma of ribonuclease P evolution.
Trends Genet: 2003, 19(10);561-9
[PubMed:14550630] [WorldCat.org] [DOI] (P p)

L A Kirsebom, A Vioque
RNase P from bacteria. Substrate recognition and function of the protein subunit.
Mol Biol Rep: 1995, 22(2-3);99-109
[PubMed:8901495] [WorldCat.org] [DOI] (P p)


Original Publications

Kyle G Daniels, Nam K Tonthat, David R McClure, Yu-Chu Chang, Xin Liu, Maria A Schumacher, Carol A Fierke, Scott C Schmidler, Terrence G Oas
Ligand concentration regulates the pathways of coupled protein folding and binding.
J Am Chem Soc: 2014, 136(3);822-5
[PubMed:24364358] [WorldCat.org] [DOI] (I p)

Alex Rosenberg, Lior Sinai, Yoav Smith, Sigal Ben-Yehuda
Dynamic expression of the translational machinery during Bacillus subtilis life cycle at a single cell level.
PLoS One: 2012, 7(7);e41921
[PubMed:22848659] [WorldCat.org] [DOI] (I p)

Christelle M Roux, Jonathon P DeMuth, Paul M Dunman
Characterization of components of the Staphylococcus aureus mRNA degradosome holoenzyme-like complex.
J Bacteriol: 2011, 193(19);5520-6
[PubMed:21764917] [WorldCat.org] [DOI] (I p)

Kristin S Koutmou, Jeremy J Day-Storms, Carol A Fierke
The RNR motif of B. subtilis RNase P protein interacts with both PRNA and pre-tRNA to stabilize an active conformer.
RNA: 2011, 17(7);1225-35
[PubMed:21622899] [WorldCat.org] [DOI] (I p)

Nicholas J Reiter, Amy Osterman, Alfredo Torres-Larios, Kerren K Swinger, Tao Pan, Alfonso Mondragón
Structure of a bacterial ribonuclease P holoenzyme in complex with tRNA.
Nature: 2010, 468(7325);784-9
[PubMed:21076397] [WorldCat.org] [DOI] (I p)

Yu-Chu Chang, William R Franch, Terrence G Oas
Probing the folding intermediate of Bacillus subtilis RNase P protein by nuclear magnetic resonance.
Biochemistry: 2010, 49(44);9428-37
[PubMed:20843005] [WorldCat.org] [DOI] (I p)

Yu-Chu Chang, Terrence G Oas
Osmolyte-induced folding of an intrinsically disordered protein: folding mechanism in the absence of ligand.
Biochemistry: 2010, 49(25);5086-96
[PubMed:20476778] [WorldCat.org] [DOI] (I p)

Kristin S Koutmou, Nathan H Zahler, Jeffrey C Kurz, Frank E Campbell, Michael E Harris, Carol A Fierke
Protein-precursor tRNA contact leads to sequence-specific recognition of 5' leaders by bacterial ribonuclease P.
J Mol Biol: 2010, 396(1);195-208
[PubMed:19932118] [WorldCat.org] [DOI] (I p)

John Hsieh, Carol A Fierke
Conformational change in the Bacillus subtilis RNase P holoenzyme--pre-tRNA complex enhances substrate affinity and limits cleavage rate.
RNA: 2009, 15(8);1565-77
[PubMed:19549719] [WorldCat.org] [DOI] (I p)

Markus Gösringer, Roland K Hartmann
Function of heterologous and truncated RNase P proteins in Bacillus subtilis.
Mol Microbiol: 2007, 66(3);801-13
[PubMed:17919279] [WorldCat.org] [DOI] (P p)

Barbara Wegscheid, Roland K Hartmann
In vivo and in vitro investigation of bacterial type B RNase P interaction with tRNA 3'-CCA.
Nucleic Acids Res: 2007, 35(6);2060-73
[PubMed:17355991] [WorldCat.org] [DOI] (I p)

Somashekarappa Niranjanakumari, Jeremy J Day-Storms, Mahiuddin Ahmed, John Hsieh, Nathan H Zahler, Ronald A Venters, Carol A Fierke
Probing the architecture of the B. subtilis RNase P holoenzyme active site by cross-linking and affinity cleavage.
RNA: 2007, 13(4);521-35
[PubMed:17299131] [WorldCat.org] [DOI] (P p)

Markus Gössringer, Rosel Kretschmer-Kazemi Far, Roland K Hartmann
Analysis of RNase P protein (rnpA) expression in Bacillus subtilis utilizing strains with suppressible rnpA expression.
J Bacteriol: 2006, 188(19);6816-23
[PubMed:16980484] [WorldCat.org] [DOI] (P p)

Christopher H Henkels, Terrence G Oas
Thermodynamic characterization of the osmolyte- and ligand-folded states of Bacillus subtilis ribonuclease P protein.
Biochemistry: 2005, 44(39);13014-26
[PubMed:16185070] [WorldCat.org] [DOI] (P p)

Christoph Rox, Ralph Feltens, Thomas Pfeiffer, Roland K Hartmann
Potential contact sites between the protein and RNA subunit in the Bacillus subtilis RNase P holoenzyme.
J Mol Biol: 2002, 315(4);551-60
[PubMed:11812129] [WorldCat.org] [DOI] (P p)

A Hansen, T Pfeiffer, T Zuleeg, S Limmer, J Ciesiolka, R Feltens, R K Hartmann
Exploring the minimal substrate requirements for trans-cleavage by RNase P holoenzymes from Escherichia coli and Bacillus subtilis.
Mol Microbiol: 2001, 41(1);131-43
[PubMed:11454206] [WorldCat.org] [DOI] (P p)

C H Henkels, J C Kurz, C A Fierke, T G Oas
Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein.
Biochemistry: 2001, 40(9);2777-89
[PubMed:11258888] [WorldCat.org] [DOI] (P p)

J M Warnecke, R Held, S Busch, R K Hartmann
Role of metal ions in the hydrolysis reaction catalyzed by RNase P RNA from Bacillus subtilis.
J Mol Biol: 1999, 290(2);433-45
[PubMed:10390342] [WorldCat.org] [DOI] (P p)

T Stams, S Niranjanakumari, C A Fierke, D W Christianson
Ribonuclease P protein structure: evolutionary origins in the translational apparatus.
Science: 1998, 280(5364);752-5
[PubMed:9563955] [WorldCat.org] [DOI] (P p)

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