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    Genetically encoding phosphotyrosine and its nonhydrolyzable analog in bacteria

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    Name:
    Genetically encoding phosphoty ...
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    Genre
    Post-print
    Date
    2017-08-01
    Author
    Luo, X
    Fu, G
    Wang, RE
    Zhu, X
    Zambaldo, C
    Liu, R
    Liu, T
    Lyu, X
    Du, J
    Xuan, W
    Yao, A
    Reed, SA
    Kang, M
    Zhang, Y
    Guo, H
    Huang, C
    Yang, PY
    Wilson, IA
    Schultz, PG
    Wang, F
    Show allShow less
    Subject
    Codon, Nonsense
    Crystallography, X-Ray
    Escherichia coli
    Ligases
    Models, Molecular
    Molecular Structure
    Phosphorylation
    Phosphotyrosine
    Recombinant Proteins
    Permanent link to this record
    http://hdl.handle.net/20.500.12613/4883
    
    Metadata
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    DOI
    10.1038/nchembio.2405
    Abstract
    © 2017 Nature America, Inc., part of Springer Nature. All rights reserved. Tyrosine phosphorylation is a common protein post-translational modification that plays a critical role in signal transduction and the regulation of many cellular processes. Using a propeptide strategy to increase cellular uptake of O-phosphotyrosine (pTyr) and its nonhydrolyzable analog 4-phosphomethyl-L-phenylalanine (Pmp), we identified an orthogonal aminoacyl-tRNA synthetase-tRNA pair that allows site-specific incorporation of both pTyr and Pmp into recombinant proteins in response to the amber stop codon in Escherichia coli in good yields. The X-ray structure of the synthetase reveals a reconfigured substrate-binding site, formed by nonconservative mutations and substantial local structural perturbations. We demonstrate the utility of this method by introducing Pmp into a putative phosphorylation site and determining the affinities of the individual variants for the substrate 3BP2. In summary, this work provides a useful recombinant tool to dissect the biological functions of tyrosine phosphorylation at specific sites in the proteome.
    Citation to related work
    Springer Science and Business Media LLC
    Has part
    Nature Chemical Biology
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    ae974a485f413a2113503eed53cd6c53
    http://dx.doi.org/10.34944/dspace/4865
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