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

scholarly journals The Dynamic Network of RNP RNase P Subunits

2021 ◽  
Vol 22 (19) ◽  
pp. 10307
Author(s):  
Athanasios-Nasir Shaukat ◽  
Eleni G. Kaliatsi ◽  
Ilias Skeparnias ◽  
Constantinos Stathopoulos
Keyword(s):  
Dynamic Network ◽  
Rnase P ◽  
Ribonuclease P ◽  
Protein Subunit ◽  
Protein Subunits ◽  
Phosphodiester Bond ◽  
Cellular Processes ◽  
Protein Partners

Ribonuclease P (RNase P) is an important ribonucleoprotein (RNP), responsible for the maturation of the 5′ end of precursor tRNAs (pre-tRNAs). In all organisms, the cleavage activity of a single phosphodiester bond adjacent to the first nucleotide of the acceptor stem is indispensable for cell viability and lies within an essential catalytic RNA subunit. Although RNase P is a ribozyme, its kinetic efficiency in vivo, as well as its structural variability and complexity throughout evolution, requires the presence of one protein subunit in bacteria to several protein partners in archaea and eukaryotes. Moreover, the existence of protein-only RNase P (PRORP) enzymes in several organisms and organelles suggests a more complex evolutionary timeline than previously thought. Recent detailed structures of bacterial, archaeal, human and mitochondrial RNase P complexes suggest that, although apparently dissimilar enzymes, they all recognize pre-tRNAs through conserved interactions. Interestingly, individual protein subunits of the human nuclear and mitochondrial holoenzymes have additional functions and contribute to a dynamic network of elaborate interactions and cellular processes. Herein, we summarize the role of each RNase P subunit with a focus on the human nuclear RNP and its putative role in flawless gene expression in light of recent structural studies.

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.

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