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

Partial activity is seen with many substitutions of highly conserved active site residues in human Pseudouridine synthase 1.

RNA (New York, N.Y.) - 1 Sept 2008

Sibert Bryan S, Fischel-Ghodsian Nathan, Patton Jeffrey R

Abstract excerpt

Pseudouridine synthase 1 (Pus1p) is an enzyme that converts uridine to Pseudouridine (Psi) in tRNA and other RNAs in eukaryotes. The active site of Pus1p is composed of stretches of amino acids that are highly conserved and it is hypothesized that mutation of select residues would impair the enzyme's ability to catalyze the formation of Psi. However, most mutagenesis studies have been confined to substitution of...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Conserved Sequence
Share to Hydro-Lyases

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

Share to Mutagenesis

Share to Nucleic Acid Conformation

Share to RNA, Transfer

Share to Substrate Specificity

Share to Tyrosine

Source

Open in PubMed Open full text

Identifiers

PMID: 18648068
DOI: 10.1261/rna.984508
PMCID: PMC2525951

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

Partial activity is seen with many substitutions of highly conserved active site residues in human Pseudouridine synthase 1.PMID 18648068Read ↗

Caenorhabditis elegans pseudouridine synthase 1 activity in vivo: tRNA is a substrate, but not U2 small nuclear RNA.Semantic proximity Read ↗

The molecular basis of tRNA selectivity by human pseudouridine synthase 3.Semantic proximity Read ↗

The yeast tRNA:pseudouridine synthase Pus1p displays a multisite substrate specificity.Semantic proximity Read ↗

Enzymatic characterization and mutational studies of TruD--the fifth family of pseudouridine synthases.Semantic proximity Read ↗

Schizosaccharomyces pombe pus1 mutants are temperature sensitive due to decay of tRNAIle(UAU) by the 5'-3' exonuclease Dhp1, primarily targeting the unspliced pre-tRNA.Semantic proximity Read ↗

The pseudouridine synthase PUSL1 modifies U39 of mitochondrial tRNAs and is linked to human neurological phenotypes.Semantic proximity Read ↗

Crystal structure of the highly divergent pseudouridine synthase TruD reveals a circular permutation of a conserved fold.Semantic proximity Read ↗

Human TRUB1 is a highly conserved pseudouridine synthase responsible for the formation of Ψ55 in mitochondrial tRNAAsn, tRNAGln, tRNAGlu and tRNAProSemantic proximity Read ↗

Mechanistic insight into the pseudouridylation of RNASemantic proximity Read ↗

The human TruB family of pseudouridine synthase genes, including the Dyskeratosis Congenita 1 gene and the novel member TRUB1Semantic proximity Read ↗

Pus1p-dependent tRNA pseudouridinylation becomes essential when tRNA biogenesis is compromised in yeast.Semantic proximity Read ↗

<i>Pus7</i> mutation links tRNA dysregulation to aggressive behavior through activation of the integrated stress response and glycolytic reprogrammingSemantic proximity Read ↗

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