Peroxin Pex21p interacts with the C-terminal noncatalytic domain of yeast seryl-tRNA synthetase and forms a specific ternary complex with tRNASer
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چکیده
منابع مشابه
Serine activation is the rate limiting step of tRNASer aminoacylation by yeast seryl tRNA synthetase.
Using the quenched flow technique the mechanism of seryl tRNA synthetase action has been investigated with respect to the presteady state kinetics of individual steps. Under conditions where the strong binding sites of the enzyme are nearly saturated and the steady state turnover number is about 1 s-1, rate constants of four different processes have been determined: steps connected with substra...
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Human cytosolic leucyl-tRNA synthetase is one component of a macromolecular aminoacyl-tRNA synthetase complex. This is unlike prokaryotic and lower eukaryotic LeuRSs that exist as free soluble enzymes. There is little known about it, since the purified enzyme has been unavailable. Herein, human cytosolic leucyl-tRNA synthetase was heterologously expressed in a baculovirus system and purified to...
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Several studies have revealed the involvement of multi aminoacyl-tRNA synthetase complexes (MSC) in archaeal and eukaryotic translation. Here we analyzed interactions of atypical Methanothermobacter thermautotrophicus seryl-tRNA synthetase (MtSerRS), transfer RNA (tRNA) and arginyl-tRNA synthetase (ArgRS). Surface plasmon resonance (SPR) was used to determine dissociation constants for the MtSe...
متن کاملThe Accuracy of Seryl-tRNA Synthesis
The high level of translational fidelity is ensured by various types of quality control mechanisms, which are adapted to prevent or correct naturally occurring mistakes. Accurate aminoacyl-tRNA synthesis is mostly dependent on the specificity of the aminoacyl-tRNA synthetases (aaRS), i.e. their ability to choose among competing structurally similar substrates. Our studies have revealed that acc...
متن کاملThe N-terminal domain of mammalian Lysyl-tRNA synthetase is a functional tRNA-binding domain.
Lysyl-tRNA synthetase from higher eukaryotes possesses a lysine-rich N-terminal polypeptide extension appended to a classical prokaryotic-like LysRS domain. Band shift analysis showed that this extra domain provides LysRS with nonspecific tRNA binding properties. A N-terminally truncated derivative of LysRS, LysRS-DeltaN, displayed a 100-fold lower apparent affinity for tRNA(3)Lys and a 3-fold ...
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ژورنال
عنوان ژورنال: FEBS Journal
سال: 2007
ISSN: 1742-464X
DOI: 10.1111/j.1742-4658.2007.05812.x