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

Lsm proteins are required for normal processing of pre-tRNAs and their efficient association with La-homologous protein Lhp1p.

Molecular and cellular biology - 1 Jul 2002

Kufel Joanna, Allmang Christine, Verdone Loredana, Beggs Jean D, Tollervey David

Abstract excerpt

Depletion of any of the five essential proteins Lsm2p to Lsm5p and Lsm8p leads to strong accumulation of all tested unspliced pre-tRNA species, as well as accumulation of 5' and 3' unprocessed species. Aberrant 3'-extended pre-tRNAs were detected, presumably due to stabilization of transcripts that fail to undergo correct transcription termination, and the accumulation of truncated tRNA fragments was also...

Read the complete abstract on PubMed

Topics

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

Share to Fungal Proteins
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ribonucleoproteins, Small Nuclear

Share to RNA-Binding Proteins

Share to RNA Precursors

Share to RNA Processing, Post-Transcriptional

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 12077351
DOI: 10.1128/MCB.22.14.5248-5256.2002
PMCID: PMC139769

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Lsm proteins are required for normal processing of pre-tRNAs and their efficient association with La-homologous protein Lhp1p.PMID 12077351Read ↗

A role for the yeast La protein in U6 snRNP assembly: evidence that the La protein is a molecular chaperone for RNA polymerase III transcripts.Semantic proximity Read ↗

Lsm Proteins are required for normal processing and stability of ribosomal RNAs.Semantic proximity Read ↗

A complex pathway for 3' processing of the yeast U3 snoRNA.Semantic proximity Read ↗

The RNA chaperone La promotes pre-tRNA maturation via indiscriminate binding of both native and misfolded targets.Semantic proximity Read ↗

Analysis of Lsm1p and Lsm8p domains in the cellular localization of Lsm complexes in budding yeast.Semantic proximity Read ↗

An intrinsically disordered C terminus allows the La protein to assist the biogenesis of diverse noncoding RNA precursors.Semantic proximity Read ↗

lsm1 mutations impairing the ability of the Lsm1p-7p-Pat1p complex to preferentially bind to oligoadenylated RNA affect mRNA decay in vivo.Semantic proximity Read ↗

U snRNP assembly in yeast involves the La protein.Semantic proximity Read ↗

The yeast La protein is required for the 3' endonucleolytic cleavage that matures tRNA precursors.Semantic proximity Read ↗

Multiple functional interactions between components of the Lsm2-Lsm8 complex, U6 snRNA, and the yeast La protein.Semantic proximity Read ↗

Mutations in the Saccharomyces cerevisiae LSM1 gene that affect mRNA decapping and 3' end protection.Semantic proximity Read ↗

Yeast Sm-like proteins function in mRNA decapping and decay.Semantic proximity Read ↗

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