Segmental isotopic labeling of a 140 kDa dimeric multi-domain protein CheA from Escherichia coli by expressed protein ligation and protein trans-splicing
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Summary
PTS approach sufficiently produced segmentally labeled ligated CheA in vivo as well as in vitro without extensive optimizations, and was less laborious than EPL approach for the routine preparation of segmentally-isotope labeled CheA dimer.
- Type
- article
- Published
- 2012-06-28
- Cited by
- 44
- References
- 48
- Access
- Open access
- OpenAlex
- https://openalex.org/W1974541397
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:16007814
Keywords
Dimer, Chemistry, Isotopic labeling, RNA splicing, Escherichia coli
References
- Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins
- Segmental Isotopic Labeling of Proteins for Nuclear Magnetic Resonance
- Improved segmental isotope labeling of proteins and application to a larger protein
- Signal transduction in bacterial chemotaxis
- Dimerization Is Required for the Activity of the Protein Histidine Kinase CheA That Mediates Signal Transduction in Bacterial Chemotaxis (*)
- Structure of the two most C‐terminal RNA recognition motifs of PTB using segmental isotope labeling
- Insights into the mechanism and catalysis of the native chemical ligation reaction.
- NMR observation of selected segments in a larger protein: central-segment isotope labeling through intein-mediated ligation.
- Site-specific labeling of proteins with NMR-active unnatural amino acids
- Intein-based biosynthetic incorporation of unlabeled protein tags into isotopically labeled proteins for NMR studies
- Crystal Structure of the CheA Histidine Phosphotransfer Domain that Mediates Response Regulator Phosphorylation in Bacterial Chemotaxis*
- Reconstruction of the chemotaxis receptor–kinase assembly
- Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element.
- Segmental isotopic labeling of multi-domain and fusion proteins by protein trans-splicing in vivo and in vitro
- Protein synthesis by native chemical ligation: expanded scope by using straightforward methodology.
- Structure of CheA, a signal-transducing histidine kinase.
- Improved Phos‐tag SDS‐PAGE under neutral pH conditions for advanced protein phosphorylation profiling
- Improved segmental isotope labeling methods for the NMR study of multidomain or large proteins: application to the RRMs of Npl3p and hnRNP L.
- Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy.
- Conformational change of H+-ATPase beta monomer revealed on segmental isotope labeling NMR spectroscopy.
Cited by
- Tandem SUMO fusion vectors for improving soluble protein expression and purification.
- Intermolecular protein splicing and its use in biotechnological applications
- Plasticity of the β-barrel assembly machinery investigated by NMR
- NMR approaches for structural analysis of multidomain proteins and complexes in solution.
- Structural basis for protein trans‐splicing by a bacterial intein‐like domain – protein ligation without nucleophilic side chains
- Structure-based engineering and comparison of novel split inteins for protein ligation†
- SPLICEFINDER – A Fast and Easy Screening Method for Active Protein Trans-Splicing Positions
- Solution structure of the two RNA recognition motifs of hnRNP A1 using segmental isotope labeling: how the relative orientation between RRMs influences the nucleic acid binding topology
- Segmental isotope‐labeling of the intrinsically disordered protein PQBP1
- Structural Studies on Inteins
- Amino Acid‐Selective Segmental Isotope Labeling of Multidomain Proteins for Structural Biology
- Semi-Synthesis of Labeled Proteins for Spectroscopic Applications
- Split-inteins and their bioapplications
- Dual modification of biomolecules.
- Segmental Isotopic Labeling of Proteins for NMR Study Using Intein Technology.
- Salt-inducible Protein Splicing in cis and trans by Inteins from Extremely Halophilic Archaea as a Novel Protein-Engineering Tool.
- Segmental Isotope Labeling of Insoluble Proteins for Solid-State NMR by Protein Trans-Splicing.
- Structural studies of potential new-generation antibiotic targets and the use of one of them, TonB as a model protein in protein engineering
- Segmental isotopic labeling of a single‐domain globular protein without any refolding step by an asparaginyl endopeptidase
- Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR
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