A Flexible peptide tether controls accessibility of a unique C-terminal RNA-binding domain in leucyl-tRNA synthetases.

doi:10.1016/j.jmb.2007.11.065

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Article

A Flexible peptide tether controls accessibility of a unique C-terminal RNA-binding domain in leucyl-tRNA synthetases.

Journal of molecular biology - 15 Feb 2008

Hsu Jennifer L, Martinis Susan A

Abstract excerpt

A unique C-terminal domain extension is required by most leucyl-tRNA synthetases (LeuRS) for aminoacylation. In one exception, the enzymatic activity of yeast mitochondrial LeuRS is actually impeded by its own C-terminal domain. It was proposed that the yeast mitochondrial LeuRS has compromised its aminoacylation activity to some extent and adapted its C terminus for a second role in RNA splicing, which is also...

Topics

Amino Acid Sequence
Aminoacylation
Bacterial Proteins
Circular Dichroism
Crystallography, X-Ray
Escherichia coli
Fungal Proteins
Gene Deletion
Genes, Bacterial
Genes, Fungal
Leucine-tRNA Ligase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mitochondria

Models, Molecular

Molecular Sequence Data

Mutagenesis, Insertional

Mutation

Peptides

Protein Structure, Tertiary

Source

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Identifiers

PMID: 18155724
DOI: 10.1016/j.jmb.2007.11.065
PMCID: PMC2270793

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