Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.26.5 extracted from

  • Walczyk, D.; Willkomm, D.K.; Hartmann, R.K.
    Bacterial type B RNase P functional characterization of the L5.1-L15.1 tertiary contact and antisense inhibition (2016), RNA, 22, 1699-1709 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.26.5

Protein Variants

Protein Variants Comment Organism
additional information L5.1-L15.1 intradomain contact in the catalytic domain of the prototypic type B RNase P RNA of Bacillus subtilis is crucial for adopting a compact functional conformation. Disruption of the L5.1-L15.1 contact by antisense oligonucleotides or mutation reduces P RNA-alone and holoenzyme activity by one to two orders of magnitude in vitro, largely retards gel mobility of the RNA and further affects the structure of regions P7/P8/P10.1, P15 and L15.2, and abolishes the ability of Bacillus subtilis P RNA to complement a P RNA-deficient Escherichia coli strain Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
additional information oligonucleotides targeting P15, but not those directed against P5.1 efficiently anneal to P RNA and inhibit activity (IC50 of about 2 nM) when incubated with preassembled Bacillus subtilis RNase P holoenzymes Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Synonyms

Synonyms Comment Organism
RNase P
-
 Bacillus subtilis