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@article{58772,
   author = {Papageorgiou, Anna and Pospíšilová, Michaela and Cibulka, Jakub and Ashraf, Raghib and Waudby, Christopher and Kadeřávek, Pavel and Maroz, Volha and Kubíček, Karel and Prokop, Zbyněk and Krejčí, Lumír and Tripsianes, Konstantinos},
   article_location = {London},
   article_number = {1},
   doi = {http://dx.doi.org/10.1038/s41467-023-42503-z},
   keywords = {Biomolecular polyelectrolyte complexes; DNA helicase Q4; G-quadruplexes; intrinsically disordered regions; RPA protein},
   language = {eng},
   issn = {2041-1723},
   journal = {Nature Communications},
   title = {Recognition and coacervation of G-quadruplexes by a multifunctional disordered region in RECQ4 helicase},
   url = {https://www.nature.com/articles/s41467-023-42503-z},
   volume = {14},
   year = {2023}
}

TY  - JOUR
ID  - 58772
AU  - Papageorgiou, Anna - Pospíšilová, Michaela - Cibulka, Jakub - Ashraf, Raghib - Waudby, Christopher - Kadeřávek, Pavel - Maroz, Volha - Kubíček, Karel - Prokop, Zbyněk - Krejčí, Lumír - Tripsianes, Konstantinos
PY  - 2023
TI  - Recognition and coacervation of G-quadruplexes by a multifunctional disordered region in RECQ4 helicase
JF  - Nature Communications
VL  - 14
IS  - 1
SP  - 1-19
EP  - 1-19
PB  - Nature Publishing Group
SN  - 2041-1723
KW  - Biomolecular polyelectrolyte complexes
KW  - DNA helicase Q4
KW  - G-quadruplexes
KW  - intrinsically disordered regions
KW  - RPA protein
UR  - https://www.nature.com/articles/s41467-023-42503-z
N2  - Biomolecular polyelectrolyte complexes can be formed between oppositely charged intrinsically disordered regions (IDRs) of proteins or between IDRs and nucleic acids. Highly charged IDRs are abundant in the nucleus, yet few have been functionally characterized. Here, we show that a positively charged IDR within the human ATP-dependent DNA helicase Q4 (RECQ4) forms coacervates with G-quadruplexes (G4s). We describe a three-step model of charge-driven coacervation by integrating equilibrium and kinetic binding data in a global numerical model. The oppositely charged IDR and G4 molecules form a complex in the solution that follows a rapid nucleation-growth mechanism leading to a dynamic equilibrium between dilute and condensed phases. We also discover a physical interaction with Replication Protein A (RPA) and demonstrate that the IDR can switch between the two extremes of the structural continuum of complexes. The structural, kinetic, and thermodynamic profile of its interactions revealed a dynamic disordered complex with nucleic acids and a static ordered complex with RPA protein. The two mutually exclusive binding modes suggest a regulatory role for the IDR in RECQ4 function by enabling molecular handoffs. Our study extends the functional repertoire of IDRs and demonstrates a role of polyelectrolyte complexes involved in G4 binding.
ER  - 

PAPAGEORGIOU, Anna, Michaela POSPÍŠILOVÁ, Jakub CIBULKA, Raghib ASHRAF, Christopher WAUDBY, Pavel KADEŘÁVEK, Volha MAROZ, Karel KUBÍČEK, Zbyněk PROKOP, Lumír KREJČÍ a Konstantinos TRIPSIANES. Recognition and coacervation of G-quadruplexes by a multifunctional disordered region in RECQ4 helicase. \textit{Nature Communications}. London: Nature Publishing Group, 2023, roč.~14, č.~1, s.~1-19. ISSN~2041-1723. Dostupné z: https://dx.doi.org/10.1038/s41467-023-42503-z.