A fifth protein subunit Ph1496p elevates the optimum temperature for the ribonuclease P activity from Pyrococcus horikoshii OT3

2006 ◽  
Vol 343 (3) ◽  
pp. 956-964 ◽  
Author(s):  
Hideo Fukuhara ◽  
Mayumi Kifusa ◽  
Mitsutoshi Watanabe ◽  
Atsushi Terada ◽  
Takashi Honda ◽  
...  
Keyword(s):  
Ribonuclease P ◽  
Optimum Temperature ◽  
Protein Subunit ◽  
Pyrococcus Horikoshii

scholarly journals Crystal structure of the ribonuclease-P-protein subunit from Staphylococcus aureus

2018 ◽  
Vol 74 (10) ◽  
pp. 632-637
Author(s):  
Lisha Ha ◽  
Jennifer Colquhoun ◽  
Nicholas Noinaj ◽  
Chittaranjan Das ◽  
Paul M. Dunman ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Staphylococcus Aureus ◽  
Rna Processing ◽  
Bacterial Species ◽  
Rna Degradation ◽  
Ribonuclease P ◽  
Protein Subunit ◽  
Aromatic Residues ◽  
Cellular Processes ◽  
P Protein

Staphylococcus aureus ribonuclease-P-protein subunit (RnpA) is a promising antimicrobial target that is a key protein component for two essential cellular processes, RNA degradation and transfer-RNA (tRNA) maturation. The first crystal structure of RnpA from the pathogenic bacterial species, S. aureus, is reported at 2.0 Å resolution. The structure presented maintains key similarities with previously reported RnpA structures from bacteria and archaea, including the highly conserved RNR-box region and aromatic residues in the precursor-tRNA 5′-leader-binding domain. This structure will be instrumental in the pursuit of structure-based designed inhibitors targeting RnpA-mediated RNA processing as a novel therapeutic approach for treating S. aureus infections.

Fluorescence properties of a tryptophan residue in an aromatic core of the protein subunit of ribonuclease P from Escherichia coli

1997 ◽  
Vol 267 (4) ◽  
pp. 765-769 ◽  
Author(s):  
Venkat Gopalan ◽  
Ralph Golbik ◽  
Gideon Schreiber ◽  
Alan R. Fersht ◽  
Sidney Altman
Keyword(s):  
Escherichia Coli ◽  
Fluorescence Properties ◽  
Ribonuclease P ◽  
Tryptophan Residue ◽  
Protein Subunit

scholarly journals Analysis of the functional role of conserved residues in the protein subunit of ribonuclease P from Escherichia coli

1997 ◽  
Vol 267 (4) ◽  
pp. 818-829 ◽  
Author(s):  
Venkat Gopalan ◽  
Andreas D Baxevanis ◽  
David Landsman ◽  
Sidney Altman
Keyword(s):  
Escherichia Coli ◽  
Functional Role ◽  
Ribonuclease P ◽  
Protein Subunit ◽  
Conserved Residues

scholarly journals Function and subnuclear distribution of Rpp21, a protein subunit of the human ribonucleoprotein ribonuclease P

RNA ◽  
2001 ◽  
Vol 7 (8) ◽  
pp. 1153-1164 ◽  
Author(s):  
NAYEF JARROUS ◽  
ROBERT REINER ◽  
DONNA WESOLOWSKI ◽  
HAGIT MANN ◽  
CECILIA GUERRIER-TAKADA ◽  
...  
Keyword(s):  
Ribonuclease P ◽  
Protein Subunit

scholarly journals The contribution of the C5 protein subunit of Escherichia coli ribonuclease P to specificity for precursor tRNA is modulated by proximal 5′ leader sequences

RNA ◽  
2017 ◽  
Vol 23 (10) ◽  
pp. 1502-1511 ◽  
Author(s):  
Courtney N. Niland ◽  
David R. Anderson ◽  
Eckhard Jankowsky ◽  
Michael E. Harris
Keyword(s):  
Escherichia Coli ◽  
Ribonuclease P ◽  
Protein Subunit

Folding of a universal ribozyme: the ribonuclease P RNA

2007 ◽  
Vol 40 (2) ◽  
pp. 113-161 ◽  
Author(s):  
Nathan J. Baird ◽  
Xing-Wang Fang ◽  
Narayanan Srividya ◽  
Tao Pan ◽  
Tobin R. Sosnick
Keyword(s):  
Rnase P ◽  
Model System ◽  
Ribonuclease P ◽  
Rna Catalysis ◽  
Protein Subunit ◽  
Catalytically Active ◽  
Ribonuclease P Rna

AbstractRibonuclease P is among the first ribozymes discovered, and is the only ubiquitously occurring ribozyme besides the ribosome. The bacterial RNase P RNA is catalytically active without its protein subunit and has been studied for over two decades as a model system for RNA catalysis, structure and folding. This review focuses on the thermodynamic, kinetic and structural frameworks derived from the folding studies of bacterial RNase P RNA.

scholarly journals Purification and characterization of Rpp25, an RNA-binding protein subunit of human ribonuclease P

RNA ◽  
2002 ◽  
Vol 8 (3) ◽  
pp. 290-295 ◽  
Author(s):  
CECILIA GUERRIER-TAKADA ◽  
PAUL S. EDER ◽  
VENKAT GOPALAN ◽  
SIDNEY ALTMAN
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Ribonuclease P ◽  
Protein Subunit ◽  
Purification And Characterization
Sign in / Sign up

Export Citation Format

Share Document