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Literature summary for 4.6.1.22 extracted from

  • Chang, Y.C.; Franch, W.R.; Oas, T.G.
    Probing the folding intermediate of Bacillus subtilis RNase P protein by nuclear magnetic resonance (2010), Biochemistry, 49, 9428-9437.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.6.1.22

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of wild-type and mutant protein P proteins in Escherichia coli strain BL21 (DE3) pLysS Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
F107W site-directed mutagenesis, pH titration experiments and comparison to the wild-type enzyme Bacillus subtilis
H105K site-directed mutagenesis, pH titration experiments and comparison to the wild-type enzyme Bacillus subtilis
H22K site-directed mutagenesis, pH titration experiments and comparison to the wild-type enzyme Bacillus subtilis
H3K site-directed mutagenesis, pH titration experiments and comparison to the wild-type enzyme Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
ribonucleoprotein RNase P protein is the protein subunit in the RNase P holoenzyme and is an intrinsically disordered protein Bacillus subtilis

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant protein P proteins from Escherichia coli strain BL21 (DE3) pLysS Bacillus subtilis

Renatured (Commentary)

Renatured (Comment) Organism
denaturing the enzyme with 6 M guanidine-HCl Bacillus subtilis

Synonyms

Synonyms Comment Organism
P protein
-
 Bacillus subtilis
ribonuclease P protein
-
 Bacillus subtilis
RNase P
-
 Bacillus subtilis

General Information

General Information Comment Organism
additional information the enzyme is conformationally heterogeneous and folds with multiphasic kinetics, indicating the presence of an equilibrium and kinetic intermediate in its folding mechanism, NMR spectroscopy analysis, overview. RNase P protein is the protein subunit in the RNase P ribonucleoholoenzyme, it is an intrinsically disordered protein. Without the binding partners, P protein is predominantly unfolded but can be induced to fold in the presence of different small anions, e.g. sulfate. The N-terminal and C-terminal helical regions are mostly unfolded in the intermediate. The protonation of His22 may play a major role in the energetics of the equilibria between the unfolded, intermediate, and folded state ensembles of P protein, possible role for the intermediate in the enzyme holoenzyme assembly process. HSQC spectrum of folded P protein and unfolded P protein, overview Bacillus subtilis