Assembly stoichiometry of bacterial selenocysteine synthase and SelC (tRNAsec)
Copyright policy )Assembly stoichiometry of bacterial selenocysteine synthase and SelC (tRNAsec)
In bacteria selenocysteyl–tRNAsec (SelC) is synthesized by selenocysteine synthase (SelA). Here we show by fluorescence anisotropy binding assays and electron microscopical symmetry analysis that the SelA–tRNAsec binding stoichiometry is of one tRNAsec molecule per SelA monomer (1:1) rather than the 1:2 value proposed previously. Negative stain transmission electron microscopy revealed a D5 pointgroup symmetry for the SelA–tRNAsec assembly both with and without tRNAsec bound. Furthermore, SelA can associate forming a supramolecular complex of stacked decamer rings, which does not occur in the presence of tRNAsec. We discuss the structure–function relationships of these assemblies and their regulatory role in bacterial selenocysteyl–tRNAsec synthesis.
- Universidade de São Paulo Brazil
- UNIVERSIDADE DE SAO PAULO Brazil
- Federal University of Rio de Janeiro Brazil
- Imperial College London United Kingdom
- Leiden University Netherlands
Base Sequence, Transcription, Genetic, Macromolecular Substances, Escherichia coli Proteins, Molecular Sequence Data, Trypanosoma brucei brucei, Fluorescence Polarization, tRNAsec, RNA, Transfer, Amino Acyl, Binding, Competitive, Stoichiometry, Selenocysteine, Kinetics, RNA, Bacterial, Selenocysteine synthase, Microscopy, Electron, Transmission, Transferases, Escherichia coli, Protein Multimerization, RNA, Protozoan, Protein Binding
Base Sequence, Transcription, Genetic, Macromolecular Substances, Escherichia coli Proteins, Molecular Sequence Data, Trypanosoma brucei brucei, Fluorescence Polarization, tRNAsec, RNA, Transfer, Amino Acyl, Binding, Competitive, Stoichiometry, Selenocysteine, Kinetics, RNA, Bacterial, Selenocysteine synthase, Microscopy, Electron, Transmission, Transferases, Escherichia coli, Protein Multimerization, RNA, Protozoan, Protein Binding
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