Function of Neurospora mitochondrial tyrosyl-tRNA synthetase in RNA splicing requires an idiosyncratic domain not found in other synthetases.

doi:10.1016/0092-8674(90)90119-y

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Article

Function of Neurospora mitochondrial tyrosyl-tRNA synthetase in RNA splicing requires an idiosyncratic domain not found in other synthetases.

Cell - 24 Aug 1990

Cherniack A D, Garriga G, Kittle J D, Akins R A, Lambowitz A M

Abstract excerpt

Neurospora mitochondrial tyrosyl-tRNA synthetase (mt TyrRS), which is encoded by nuclear gene cyt-18, functions in splicing group I introns. Analysis of intragenic partial revertants of the cyt-18-2 mutant and in vitro mutants of the cyt-18 protein expressed in E. coli showed that splicing activity of the cyt-18 protein is dependent on a small N-terminal domain that has no homolog in bacterial or yeast mt TyrRSs....

Topics

Amino Acid Sequence
Amino Acyl-tRNA Synthetases
Base Sequence
Genes, Fungal
Mitochondria
Molecular Sequence Data
Molecular Weight
Mutation
Neurospora
Neurospora crassa
Phenotype

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Conformation

RNA Splicing

Spectrum Analysis

Structure-Activity Relationship

Tyrosine

Tyrosine-tRNA Ligase

Source

Open in PubMed

Identifiers

PMID: 2143700
DOI: 10.1016/0092-8674(90)90119-y

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2143700-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Function of Neurospora mitochondrial tyrosyl-tRNA synthetase in RNA splicing requires an idiosyncratic domain not found in other synthetases.PMID 2143700Read ↗

A tyrosyl-tRNA synthetase suppresses structural defects in the two major helical domains of the group I intron catalytic core.Semantic proximity Read ↗

The Neurospora crassa CYT-18 protein C-terminal RNA-binding domain helps stabilize interdomain tertiary interactions in group I introns.Semantic proximity Read ↗

A ribosomal function is necessary for efficient splicing of the T4 phage thymidylate synthase intron in vivo.Semantic proximity Read ↗

A DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing.Semantic proximity Read ↗

Function of tyrosyl-tRNA synthetase in splicing group I introns: an induced-fit model for binding to the P4-P6 domain based on analysis of mutations at the junction of the P4-P6 stacked helices.Semantic proximity Read ↗

The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function.Semantic proximity Read ↗

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RNA chaperone StpA loosens interactions of the tertiary structure in the td group I intron in vivo.Semantic proximity Read ↗

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