A peptide affinity reagent for isolating an intact and catalytically active multi-protein complex from mammalian cells. Saathoff, H., Brofelth, M., Trinh, A., Parker, B., L., Ryan, D., P., Low, J., K., Webb, S., R., Silva, A., P., Mackay, J., P., & Shepherd, N., E. Bioorganic & Medicinal Chemistry, 23(5):960-965, 3, 2015. ![A peptide affinity reagent for isolating an intact and catalytically active multi-protein complex from mammalian cells [link]](https://bibbase.org/img/filetypes/link.svg "link")
Website doi abstract bibtex 1 download We have developed an approach for directly isolating an intact multi-protein chromatin remodeling complex from mammalian cell extracts using synthetic peptide affinity reagent 4. FOG1(1-15), a short peptide sequence known to target subunits of the nucleosome remodeling and deacetylase (NuRD) complex, was joined via a 35-atom hydrophilic linker to the StreptagII peptide. Loading this peptide onto Streptactin beads enabled capture of the intact NuRD complex from MEL cell nuclear extract. Gentle biotin elution yielded the desired intact complex free of significant contaminants and in a form that was catalytically competent in a nucleosome remodeling assay. The efficiency of 4 in isolating the NuRD complex was comparable to other reported methods utilising recombinantly produced GST-FOG1(1-45).
@article{
title = {A peptide affinity reagent for isolating an intact and catalytically active multi-protein complex from mammalian cells},
type = {article},
year = {2015},
keywords = {Affinity purification,Friend of GATA1 (FOG1),Multi-protein complex,Nucleosome remodeling and deacetylase complex pept},
pages = {960-965},
volume = {23},
websites = {https://linkinghub.elsevier.com/retrieve/pii/S0968089615000395},
month = {3},
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read = {false},
starred = {false},
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confirmed = {true},
hidden = {false},
citation_key = {Saathoff2015},
source_type = {ARTICLE},
notes = {cited By 5},
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abstract = {We have developed an approach for directly isolating an intact multi-protein chromatin remodeling complex from mammalian cell extracts using synthetic peptide affinity reagent 4. FOG1(1-15), a short peptide sequence known to target subunits of the nucleosome remodeling and deacetylase (NuRD) complex, was joined via a 35-atom hydrophilic linker to the StreptagII peptide. Loading this peptide onto Streptactin beads enabled capture of the intact NuRD complex from MEL cell nuclear extract. Gentle biotin elution yielded the desired intact complex free of significant contaminants and in a form that was catalytically competent in a nucleosome remodeling assay. The efficiency of 4 in isolating the NuRD complex was comparable to other reported methods utilising recombinantly produced GST-FOG1(1-45).},
bibtype = {article},
author = {Saathoff, Hinnerk and Brofelth, Mattias and Trinh, Anne and Parker, Benjamin L. and Ryan, Daniel P. and Low, Jason K.K. and Webb, Sarah R. and Silva, Ana P.G. and Mackay, Joel P. and Shepherd, Nicholas E.},
doi = {10.1016/j.bmc.2015.01.023},
journal = {Bioorganic & Medicinal Chemistry},
number = {5}
}
Downloads: 1
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