Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Contributions of phylogenetically variable structural elements to the function of the ribozyme ribonuclease P.

Biochemistry - 21 Jan 1992

Darr S C, Zito K, Smith D, Pace N R

Abstract excerpt

Ribonuclease P (RNase P) is a ribonucleoprotein enzyme which participates in processing precursor tRNAs. The RNA subunit contains the catalytic site and is capable of catalysis in the absence of the protein subunit. RNase P RNAs from various eubacteria consist of a core of conserved sequence and secondary structure which is evolutionarily modified in different organisms by the presence of discrete helical...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Base Sequence
Share to Escherichia coli Proteins
Share to Genetic Variation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Kinetics

Share to Molecular Sequence Data

Share to Nucleic Acid Conformation

Share to Phylogeny

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 1370627
DOI: 10.1021/bi00117a003

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Contributions of phylogenetically variable structural elements to the function of the ribozyme ribonuclease P.PMID 1370627Read ↗

Contribution of structural elements to Thermus thermophilus ribonuclease P RNA function.Semantic proximity Read ↗

Evolutionary variation in bacterial RNase P RNAs.Semantic proximity Read ↗

Minor changes largely restore catalytic activity of archaeal RNase P RNA from Methanothermobacter thermoautotrophicus.Semantic proximity Read ↗

G350 of Escherichia coli RNase P RNA contributes to Mg2+ binding near the active site of the enzyme.Semantic proximity Read ↗

Insight into the functional role of unique determinants in RNA component of RNase P of Mycobacterium tuberculosis.Semantic proximity Read ↗

Type A and B RNase P RNAs are interchangeable in vivo despite substantial biophysical differences.Semantic proximity Read ↗

Mutation of the gene encoding the ribonuclease P RNA in the hyperthermophilic archaeon Thermococcus kodakarensis causes decreased growth rate and impaired processing of tRNA precursors.Semantic proximity Read ↗

In vitro selection of RNase P RNA reveals optimized catalytic activity in a highly conserved structural domain.Semantic proximity Read ↗

Two distinct regions on the surface of an RNA-binding domain are crucial for RNase E function.Semantic proximity Read ↗

Recognition of the 5' leader of pre-tRNA substrates by the active site of ribonuclease P.Semantic proximity Read ↗

Characterization of conserved sequence elements in eukaryotic RNase P RNA reveals roles in holoenzyme assembly and tRNA processing.Semantic proximity Read ↗

The RNR motif of B. subtilis RNase P protein interacts with both PRNA and pre-tRNA to stabilize an active conformer.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.