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

Effects of conserved D/T loop substitutions in the pre-tRNA substrate on tRNase Z catalysis.

RNA biology - 1 Jan 2000

Hopkinson Angela, Levinger Louis

Abstract excerpt

tRNAs are transcribed as precursors with a 5' end leader and a 3' end trailer. In the course of tRNA maturation, RNase P removes the 5' end leader and tRNase Z can endonucleolytically remove the 3' end trailer. A domain remote from the active site of tRNase Z recognizes and binds substrate, principally through contacts with the elbow (D/T loops) of the tRNA. To evaluate possible contacts, processing kinetics was...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus subtilis
Share to Catalysis
Share to Conserved Sequence

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

Share to Endoribonucleases

Share to Nucleic Acid Conformation

Share to RNA Precursors

Share to RNA Processing, Post-Transcriptional

Share to Substrate Specificity

Source

Identifiers

PMID: 18421255
DOI: 10.4161/rna.5.2.6086

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

Effects of conserved D/T loop substitutions in the pre-tRNA substrate on tRNase Z catalysis.PMID 18421255Read ↗

Effect of changes in the flexible arm on tRNase Z processing kinetics.Semantic proximity Read ↗

Naturally occurring mutations in human mitochondrial pre-tRNASer(UCN) can affect the transfer ribonuclease Z cleavage site, processing kinetics, and substrate secondary structure.Semantic proximity Read ↗

Pathogenesis-related mutations in the T-loops of human mitochondrial tRNAs affect 3' end processing and tRNA structure.Semantic proximity Read ↗

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

Residues in the conserved His domain of fruit fly tRNase Z that function in catalysis are not involved in substrate recognition or binding.Semantic proximity Read ↗

The effects of matrices of paired substitutions in mid-acceptor stem on Drosophila tRNA(His) structure and end-processing.Semantic proximity Read ↗

The kinetics and specificity of cleavage by RNase P is mainly dependent on the structure of the amino acid acceptor stem.Semantic proximity Read ↗

Analysis of the functional modules of the tRNA 3' endonuclease (tRNase Z).Semantic proximity Read ↗

Pathology-related substitutions in human mitochondrial tRNA(Ile) reduce precursor 3' end processing efficiency in vitro.Semantic proximity Read ↗

The exocyclic amine at the RNase P cleavage site contributes to substrate binding and catalysis.Semantic proximity Read ↗

The flexible arm of tRNase Z is not essential for pre-tRNA binding but affects cleavage site selection.Semantic proximity Read ↗

The processing of wild type and mutant forms of rat nuclear pre-tRNA(Lys) by the homologous RNase P.Semantic proximity Read ↗

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