DNA Tile Self-Assembly Guided by Base Excision Repair Enzymes.

DNA Nanotechnology DNA Repair Enzymes DNA Structures DNA Tiles Self-Assembly

Journal

Angewandte Chemie (International ed. in English)
ISSN: 1521-3773
Titre abrégé: Angew Chem Int Ed Engl
Pays: Germany
ID NLM: 0370543

Informations de publication

Date de publication:
22 08 2022
Historique:
received: 07 06 2022
pubmed: 29 6 2022
medline: 19 8 2022
entrez: 28 6 2022
Statut: ppublish

Résumé

We demonstrate here the use of DNA repair enzymes to control the assembly of DNA-based structures. To do so, we employed uracil-DNA glycosylase (UDG) and formamidopyrimidine DNA glycosylase (Fpg), two enzymes involved in the base excision repair (BER) pathway. We designed two responsive nucleic acid modules containing mutated bases (deoxyuridine or 8-oxo-7,8-dihydroguanine recognized by UDG and Fpg, respectively) that, upon the enzyme repair activity, release a nucleic acid strand that induces the self-assembly of DNA tiles into tubular structures. The approach is programmable, specific and orthogonal and the two responsive modules can be used in the same solution without crosstalk. This allows to assemble structures formed by two different tiles in which the tile distribution can be accurately predicted as a function of the relative activity of each enzyme. Finally, we show that BER-enzyme inhibitors can also be used to control DNA-tile assembly in a specific and concentration-dependent manner.

Identifiants

pubmed: 35762986
doi: 10.1002/anie.202208367
doi:

Substances chimiques

DNA 9007-49-2
Uracil-DNA Glycosidase EC 3.2.2.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

e202208367

Informations de copyright

© 2022 Wiley-VCH GmbH.

Références

N. Chatterjee, G. C. Walker, Environ. Mol. Mutagen. 2017, 58, 235-263.
T. Helleday, E. Petermann, C. Lundin, B. Hodgson, R. A. Sharma, Nat. Rev. Cancer 2008, 8, 193-204.
A. Ciccia, S. J. Elledge, Mol. Cell 2010, 40, 179-204.
A. Sancar, L. A. Lindsey-Boltz, K. Ünsal-Kaçmaz, S. Linn, Annu. Rev. Biochem. 2004, 73, 39-85.
H. E. Krokan, M. Bjørås, Cold Spring Harbor Perspect. Biol. 2013, 5, a012583.
M. L. Hegde, T. K. Hazra, S. Mitra, Cell Res. 2008, 18, 27-47.
S. D. Bruner, D. P. G. Norman, G. L. Verdine, Nature 2000, 403, 859-866.
S. S. David, V. L. O'Shea, S. Kundu, Nature 2007, 447, 941-950.
A. L. Jacobs, P. Schär, Chromosoma 2012, 121, 1-20.
T. Visnes, A. Cázares-Körner, W. Hao, O. Wallner, G. Masuyer, O. Loseva, O. Mortusewicz, E. Wiita, A. Sarno, A. Manoilov, J. Astorga-Wells, A. S. Jemth, L. Pan, K. Sanjiv, S. Karsten, C. Gokturk, M. Grube, E. J. Homan, B. M. F. Hanna, C. B. J. Paulin, T. Pham, A. Rasti, U. W. Berglund, C. Von Nicolai, C. Benitez-Buelga, T. Koolmeister, D. Ivanic, P. Iliev, M. Scobie, H. E. Krokan, P. Baranczewski, P. Artursson, M. Altun, A. J. Jensen, C. Kalderén, X. Ba, R. A. Zubarev, P. Stenmark, I. Boldogh, T. Helleday, Science 2018, 362, 834-839.
N. J. Curtin, Nat. Rev. Cancer 2012, 12, 801-817.
N. Farag, R. Mattossovich, R. Merlo, Ł. Nierzwicki, G. Palermo, A. Porchetta, G. Perugino, F. Ricci, Angew. Chem. Int. Ed. 2021, 60, 7283-7289;
Angew. Chem. 2021, 133, 7359-7365.
D. L. Wilson, E. T. Kool, J. Am. Chem. Soc. 2019, 141, 19379-19388.
T. Ono, S. Wang, C.-K. Koo, L. Engstrom, S. S. David, E. T. Kool, Angew. Chem. Int. Ed. 2012, 51, 1689-1692;
Angew. Chem. 2012, 124, 1721-1724.
N. C. Seeman, H. F. Sleiman, Nat. Rev. Mater. 2017, 3, 17068.
M. Lin, J. Wang, G. Zhou, J. Wang, N. Wu, J. Lu, J. Gao, X. Chen, J. Shi, X. Zuo, C. Fan, Angew. Chem. Int. Ed. 2015, 54, 2151-2155;
Angew. Chem. 2015, 127, 2179-2183.
S. Ranallo, A. Porchetta, F. Ricci, Anal. Chem. 2019, 91, 44-59.
S. Gentile, E. Del Grosso, L. J. Prins, F. Ricci, Angew. Chem. Int. Ed. 2021, 60, 12911-12917;
Angew. Chem. 2021, 133, 13021-13027.
P. Chidchob, D. Offenbartl-Stiegert, D. McCarthy, X. Luo, J. Li, S. Howorka, H. F. Sleiman, J. Am. Chem. Soc. 2019, 141, 1100-1108.
H. Ramezani, H. Dietz, Nat. Rev. Genet. 2020, 21, 5-26.
S. Gentile, E. Del Grosso, P. E. Pungchai, E. Franco, L. J. Prins, F. Ricci, J. Am. Chem. Soc. 2021, 143, 20296-20301.
M. Pfeiffer, K. Trofymchuk, S. Ranallo, F. Ricci, F. Steiner, F. Cole, V. Glembockyte, P. Tinnefeld, iScience 2021, 24, 103072.
E. Del Grosso, L. J. Prins, F. Ricci, Angew. Chem. Int. Ed. 2020, 59, 13238-13245;
Angew. Chem. 2020, 132, 13340-13347.
A. Amodio, E. Del Grosso, A. Troina, E. Placidi, F. Ricci, Nano Lett. 2018, 18, 2918-2923.
S. W. Schaffter, L. N. Green, J. Schneider, H. K. K. Subramanian, R. Schulman, E. Franco, Nucleic Acids Res. 2018, 46, 5332-5343.
D. Y. Zhang, G. Seelig, Nat. Chem. 2011, 3, 103-113.
H. Zhang, Y. Wang, H. Zhang, X. Liu, A. Lee, Q. Huang, F. Wang, J. Chao, H. Liu, J. Li, J. Shi, X. Zuo, L. Wang, L. Wang, X. Cao, C. Bustamante, Z. Tian, C. Fan, Nat. Commun. 2019, 10, 1006.
M. Langecker, V. Arnaut, T. G. Martin, J. List, S. Renner, M. Mayer, H. Dietz, F. C. Simmel, Science 2012, 338, 932-936.
B. Saccà, R. Meyer, M. Erkelenz, K. Kiko, A. Arndt, H. Schroeder, K. S. Rabe, C. M. Niemeyer, B. Saccà, D.-C. R. Meyer, D.-B. M. Erkelenz, M. K. Sc Kiko, A. Arndt, H. Schroeder, K. S. Rabe, C. M. Niemeyer, Angew. Chem. Int. Ed. 2010, 49, 9378-9383;
Angew. Chem. 2010, 122, 9568-9573.
S. Ranallo, D. Sorrentino, F. Ricci, Nat. Commun. 2019, 10, 5509.
L. N. Green, A. Amodio, H. K. K. Subramanian, F. Ricci, E. Franco, Nano Lett. 2017, 17, 7283-7288.
A. Amodio, A. F. Adedeji, M. Castronovo, E. Franco, F. Ricci, J. Am. Chem. Soc. 2016, 138, 12735-12738.
V. A. Turek, R. Chikkaraddy, S. Cormier, B. Stockham, T. Ding, U. F. Keyser, J. J. Baumberg, V. A. Turek, R. Chikkaraddy, S. Cormier, B. Stockham, T. Ding, U. F. Keyser, J. J. Baumberg, Adv. Funct. Mater. 2018, 28, 1706410.
A. Kuzyk, Y. Yang, X. Duan, S. Stoll, A. O. Govorov, H. Sugiyama, M. Endo, N. Liu, Nat. Commun. 2016, 7, 10591.
E. M. Willner, Y. Kamada, Y. Suzuki, T. Emura, K. Hidaka, H. Dietz, H. Sugiyama, M. Endo, Angew. Chem. Int. Ed. 2017, 56, 15324-15328;
Angew. Chem. 2017, 129, 15526-15530.
K. Jahnke, V. Huth, U. Mersdorf, N. Liu, K. Göpfrich, ACS Nano 2022, 16, 7233-7241.
P. W. K. Rothemund, A. Ekani-Nkodo, N. Papadakis, A. Kumar, D. K. Fygenson, E. Winfree, J. Am. Chem. Soc. 2004, 126, 16344-16352.
D. Y. Zhang, R. F. Hariadi, H. M. T. Choi, E. Winfree, Nat. Commun. 2013, 4, 1965.
L. N. Green, H. K. K. Subramanian, V. Mardanlou, J. Kim, R. F. Hariadi, E. Franco, Nat. Chem. 2019, 11, 510-520.
N. Schormann, R. Ricciardi, D. Chattopadhyay, Protein Sci. 2014, 23, 1667-1685.
S. Van Der Veen, C. M. Tang, Nat. Rev. Microbiol. 2015, 13, 83-94.
S. Boiteux, F. Coste, B. Castaing, Free Radical Biol. Med. 2017, 107, 179-201.
P. Handa, S. Roy, U. Varshney, J. Biol. Chem. 2001, 276, 17324-17331.
S. S. Parikh, C. D. Putnam, J. A. Tainer, Mutat. Res. 2000, 460, 183-199.
A. Biela, F. Coste, F. Culard, M. Guerin, S. Goffinont, K. Gasteiger, J. Cies̈la, A. Winczura, Z. Kazimierczuk, D. Gasparutto, T. Carell, B. Tudek, B. Castaing, Nucleic Acids Res. 2014, 42, 10748.
C. Rieux, S. Goffinont, F. Coste, Z. Tber, J. Cros, V. Roy, M. Guérin, V. Gaudon, S. Bourg, A. Biela, V. Aucagne, L. Agrofoglio, N. Garnier, B. Castaing, Int. J. Mol. Sci. 2020, 21, 2058.
J. M. Stewart, M. Viard, H. K. K. Subramanian, B. K. Roark, K. A. Afonin, E. Franco, Nanoscale 2016, 8, 17542-17550.
A. R. Chandrasekaran, Nanoscale 2016, 8, 4436-4446.
J. Mikkilä, A. P. Eskelinen, E. H. Niemelä, V. Linko, M. J. Frilander, P. Törmä, M. A. Kostiainen, Nano Lett. 2014, 14, 2196-2200.
Y. X. Zhao, A. Shaw, X. Zeng, E. Benson, A. M. Nyström, B. Högberg, ACS Nano 2012, 6, 8684-8691.
S. Sagredo, T. Pirzer, A. AghebatRafat, M. A. Goetzfried, G. Moncalian, F. C. Simmel, F. De La Cruz, Angew. Chem. Int. Ed. 2016, 55, 4348-4352;
Angew. Chem. 2016, 128, 4421-4425.
W. P. Klein, R. P. Thomsen, K. B. Turner, S. A. Walper, J. Vranish, J. Kjems, M. G. Ancona, I. L. Medintz, ACS Nano 2019, 13, 13677-13689.
C. Sigl, E. M. Willner, W. Engelen, J. A. Kretzmann, K. Sachenbacher, A. Liedl, F. Kolbe, F. Wilsch, S. A. Aghvami, U. Protzer, M. F. Hagan, S. Fraden, H. Dietz, Nat. Mater. 2021, 20, 1281-1289.
Z. Zhang, Y. Yang, F. Pincet, M. C. Llaguno, C. Lin, Nat. Chem. 2017, 9, 653-659.

Auteurs

Nada Farag (N)

Department of Chemical Sciences and Technologies, University of Rome Tor Vergata, Via della Ricerca Scientifica, 00133, Rome, Italy.

Gianfranco Ercolani (G)

Department of Chemical Sciences and Technologies, University of Rome Tor Vergata, Via della Ricerca Scientifica, 00133, Rome, Italy.

Erica Del Grosso (E)

Department of Chemical Sciences and Technologies, University of Rome Tor Vergata, Via della Ricerca Scientifica, 00133, Rome, Italy.

Francesco Ricci (F)

Department of Chemical Sciences and Technologies, University of Rome Tor Vergata, Via della Ricerca Scientifica, 00133, Rome, Italy.

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