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@article{38921,
   author = {Brázda, Pavel and Šedo, Ondrej and Kubíček, Karel and Štefl, Richard},
   article_location = {UNITED HOUSE, 2 ALBERT PL, LONDON N3 1QB},
   article_number = {1},
   keywords = {C-terminal domain; co-expression; CTD; IDP; intrinsically disordered proteins; phosphorylation; purification; RNA polymerase II; TRANSCRIPTION TERMINATION; LARGEST SUBUNIT; CELL-CYCLE; KINASE; STRATEGIES; SEMISYNTHESIS},
   language = {eng},
   issn = {0736-6205},
   journal = {BioTechniques},
   title = {Efficient and robust preparation of tyrosine phosphorylated intrinsically disordered proteins},
   url = {https://www.future-science.com/doi/full/10.2144/btn-2019-0033},
   volume = {67},
   year = {2019}
}

TY  - JOUR
ID  - 38921
AU  - Brázda, Pavel - Šedo, Ondrej - Kubíček, Karel - Štefl, Richard
PY  - 2019
TI  - Efficient and robust preparation of tyrosine phosphorylated intrinsically disordered proteins
JF  - BioTechniques
VL  - 67
IS  - 1
SP  - 16-22
EP  - 16-22
PB  - FUTURE SCI LTD
SN  - 0736-6205
KW  - C-terminal domain
KW  - co-expression
KW  - CTD
KW  - IDP
KW  - intrinsically disordered proteins
KW  - phosphorylation
KW  - purification
KW  - RNA polymerase II
KW  - TRANSCRIPTION TERMINATION
KW  - LARGEST SUBUNIT
KW  - CELL-CYCLE
KW  - KINASE
KW  - STRATEGIES
KW  - SEMISYNTHESIS
UR  - https://www.future-science.com/doi/full/10.2144/btn-2019-0033
N2  - Intrinsically disordered proteins (IDPs) are subject to post-translational modifications. This allows the same polypeptide to undertake different interaction networks with different consequences, ranging from regulatory signalling networks to formation of membraneless organelles. We report a robust method for co-expression of modification enzyme and SUMO-tagged IDP with subsequent purification procedure allowing production of modified IDP. The robustness of our protocol is demonstrated on a challenging system, RNA polymerase II C-terminal domain (CM), that is a low-complexity repetitive region with multiple phosphorylation sites. In vitro phosphorylation approaches fail to yield multiple-site phosphorylated CTD, whereas our in vivo protocol allows to rapidly produce near homogeneous phosphorylated CTD at a low cost. These samples can be used in functional and structural studies.
ER  - 

BRÁZDA, Pavel, Ondrej ŠEDO, Karel KUBÍČEK a Richard ŠTEFL. Efficient and robust preparation of tyrosine phosphorylated intrinsically disordered proteins. \textit{BioTechniques}. UNITED HOUSE, 2 ALBERT PL, LONDON N3 1QB: FUTURE SCI LTD, 2019, roč.~67, č.~1, s.~16-22. ISSN~0736-6205.