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

Comparative study on tertiary contacts and folding of RNase P RNAs from a psychrophilic, a mesophilic/radiation-resistant, and a thermophilic bacterium.

RNA (New York, N.Y.) - 1 Oct 2021

Marszalkowski Michal, Werner Andreas, Feltens Ralph, Helmecke Dominik, Gößringer Markus, Westhof Eric, Hartmann Roland K

Abstract excerpt

In most bacterial type A RNase P RNAs (P RNAs), two major loop-helix tertiary contacts (L8-P4 and L18-P8) help to orient the two independently folding S- and C-domains for concerted recognition of precursor tRNA substrates. Here, we analyze the effects of mutations in these tertiary contacts in P RNAs from three different species: (i) the psychrophilic bacterium Pseudoalteromonas translucida (Ptr), (ii) the...

Read the complete abstract on PubMed

Topics

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

Share to Base Pairing
Share to Deinococcus

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

Share to Ribonuclease P

Share to RNA, Bacterial

Share to RNA Folding

Share to RNA Stability

Share to RNA, Transfer

Share to Thermus thermophilus

Source

Open in PubMed Open full text

Identifiers

PMID: 34266994
DOI: 10.1261/rna.078735.121
PMCID: PMC8457005

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

Comparative study on tertiary contacts and folding of RNase P RNAs from a psychrophilic, a mesophilic/radiation-resistant, and a thermophilic bacterium.PMID 34266994Read ↗

Interplay between the trigger loop and the F loop during RNA polymerase catalysis.Semantic proximity Read ↗

Allosteric control of catalysis by the F loop of RNA polymerase.Semantic proximity Read ↗

Cooperative RNP assembly: complementary rescue of structural defects by protein and RNA subunits of archaeal RNase P.Semantic proximity Read ↗

Single-molecule transition-state analysis of RNA folding.Semantic proximity Read ↗

Thermodynamic analysis of a multifunctional RNA-binding protein, PhoRpp38, in the hyperthermophilic archaeon Pyrococcus horikoshii OT3.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 ↗

Identification of thermodynamically relevant interactions between EF-Tu and backbone elements of tRNA.Semantic proximity Read ↗

Structural basis of the enhanced stability of a mutant ribozyme domain and a detailed view of RNA--solvent interactions.Semantic proximity Read ↗

Temperature-responsive in vitro RNA structurome of <i>Yersinia pseudotuberculosis</i>Semantic proximity Read ↗

Multiple unfolding events during native folding of the Tetrahymena group I ribozyme.Semantic proximity Read ↗

Comparative study of two box H/ACA ribonucleoprotein pseudouridine-synthases: relation between conformational dynamics of the guide RNA, enzyme assembly and activity.Semantic proximity Read ↗

A general method for rapid and nondenaturing purification of RNAs.Semantic proximity Read ↗

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