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Showing 1 to 7 of 7 for “"CP1 domain"”.
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CP1 domain of leucyl-tRNA synthetase: dissecting its dual roles in amino acid editing and RNA splicing
Item marked as restricted to the 'Administrator' Group (id=1) by William Ingram (wingram2@illinois.edu) on 2012-06-27T21:32:36Z Item is restricted until 2014-06-27T21:32:23Z
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Characterization of Molecular Structure-Function Relationships of Escherichia Coli Leucyl-Trna Synthetase
… large module called the connective peptide 1 (CP1) domain to correct its mistakes via a hydrolytic amino acid editing mechanism. Surprisingly, deletion of the CP1 domain from Escherichia coli LeuRS yielded a catalytic core that retains fidelity. This suggests that deletion of the CP1 domain may …
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Editing by leucyl-trna synthetase: Discrimination of norvaline and isoleucine
… or by hydrolyzing mischarged amino acids in the CP1 editing domain. The enzyme’s dependence between the two editing mechanisms can shift based on the origin from which the AARS is derived, the amino acid that is targeted for editing, or presence of a mutation in the enzyme. In the absence of the …
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Mechanisms of leucyl-tRNA synthetase dependent group I intron splicing
… have been isolated within the amino acid editing CP1 domain and restore native RNA splicing activity in the presence of an inactive maturase. Mutational analysis of these sites and the regions that surround them demonstrated that certain substitutions can also inactivate LeuRS-dependent splicing …
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Biochemical Analysis of the Molecular Factors of Leucyl-Trna Synthetase That Ensure Aminoacylation Fidelity
… editing active site within a completely separate domain called CP1. A peptide has been identified within the CP1 domain of Escherichia coli (E. coli) LeuRS, which is distal to the hydrolytic editing active site, and contributes to translocation of mischarged tRNA products. Mutational analysis of …
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Leucyl-tRNA synthetase: dynamic subcellular relocalization and drug resistance mechanism
… tRNALeu in the editing site of the enzyme’s CP1 domain. Some resistant mutations are located outside of the CP1 hydrolytic editing active site. Thus, their mode of action was not understood. A combination of X-ray crystallography, molecular dynamics, biochemical experiments, and mutational …
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Characterization of leucyl-TRNA synthetase from homo sapiens and escherichia coli in aminoacylation, amino acid editing and interdomain interactions
… editing active site that resides in a discrete domain called the connective polypeptide 1 domain (CP1). Post-transfer editing involves the translocation of mischarged tRNA from the aminoacylation to the editing active site where mischarged tRNA binds for hydrolysis of the noncognate amino acid …