Publications

Selected:
* Corresponding author

Dubiez, E., Pellegrini, E., Finderup Brask M., Garland, W., Foucher, A.-E., Huard, K., Jensen, T.H, Cusack, S.* and Kadlec, J.* Structural basis for competitive binding of productive and degradative co-transcriptional effectors to the nuclear cap-binding complex.
Cell Rep 43:113639 (2024)

Laroussi, H., Juarez-Martinez, A.B., Le Roy, A., Boeri Erba, E., Gabel, F., de Massy, B. and Kadlec, J. Characterization of the REC114-MEI4-IHO1 complex regulating meiotic DNA double-strand break formation. EMBO J. 42: e113866 (2023)

Foucher, A.-E., Touat-Todeschini, L., Juarez-Martinez, A.B., Rakitch, A., Laroussi, H., Karczewski, C., Acajjaoui, S., Soler-López, M., Cusack, S., Mackereth, C.D.*, Verdel, A.* and Kadlec, J.* Structural analysis of Red1 as a conserved scaffold of the RNA-targeting MTREC/PAXT complex.
Nat. Commun. 13, 4969 (2022).

Nore, A., Juarez-Martinez, A.B., Clément, J., Brun, C., Diagouraga, B., Laroussi, H., Grey, C., Bourbon, H.M., Kadlec, J.*, Robert, T*. and de Massy, B.* TOPOVIBL-REC114 interaction regulates meiotic DNA double-strand breaks. Nat. Commun. 13:7048 (2022)

Dias, J., Nguyen, N., Georgiev, P., Gaub, A., Brettschneider, J., Cusack, S., Kadlec, J.* and Akhtar, A.* Structural analysis of the KANSL1/WDR5/KANSL2 complex reveals that WDR5 is required for efficient assembly and chromatin targeting of the NSL complex.
Genes Dev. 28: 929-942 (2014)

Wu, H., Mathioudakis, N., Diagouraga, B., Dong A., Dombrovski, L., Baudat. F., Cusack, S., de Massy, B.* and Kadlec, J.* Molecular basis for the regulation of the H3K4 methyltransferase activity of PRDM9. Cell Rep. 5:13-20 (2013)

Hallacli, E., Lipp, M., Georgiev, P., Spielman, C., Cusack, S., Akhtar, A.* and Kadlec, J.* MSL1-mediated dimerization of the dosage compensation complex is essential for male X-chromosome regulation in Drosophila. Mol. Cell 48:587-600 (2012)

All:
Dubiez, E., Pellegrini, E., Finderup Brask M., Garland, W., Foucher, A.-E., Huard, K., Jensen, T.H, Cusack, S.* and Kadlec, J.* Structural basis for competitive binding of productive and degradative co-transcriptional effectors to the nuclear cap-binding complex.
Cell Rep 43:113639 (2024)

Laroussi, H., Juarez-Martinez, A.B., Le Roy, A., Boeri Erba, E., Gabel, F., de Massy, B. and Kadlec, J. Characterization of the REC114-MEI4-IHO1 complex regulating meiotic DNA double-strand break formation. EMBO J. 42: e113866 (2023)

Foucher, A.-E., Touat-Todeschini, L., Juarez-Martinez, A.B., Rakitch, A., Laroussi, H., Karczewski, C., Acajjaoui, S., Soler-López, M., Cusack, S., Mackereth, C.D.*, Verdel, A.* and Kadlec, J.* Structural analysis of Red1 as a conserved scaffold of the RNA-targeting MTREC/PAXT complex.
Nat. Commun. 13, 4969 (2022).

Nore, A., Juarez-Martinez, A.B., Clément, J., Brun, C., Diagouraga, B., Laroussi, H., Grey, C., Bourbon, H.M., Kadlec, J.*, Robert, T*. and de Massy, B.* TOPOVIBL-REC114 interaction regulates meiotic DNA double-strand breaks. Nat. Commun. 13:7048 (2022)

Mann, N., Mzoughi, S., Schneider, R., Kühl, S.J., Schanze, D., Klämbt, V., Lovric, S., Mao, Y., Shi, S., Tan, W., Kühl, M., Onuchic-Whitford, A.C., Treimer, E., Kitzler, T.M., Kause, F., Schumann, S., Nakayama, M., Buerger, F., Shril, S., van der Ven, A.T., Majmundar, A.J., Holton, K.M., Kolb, A., Braun, D.A., Rao, J., Jobst-Schwan, T., Mildenberger, E., Lennert, T., Kuechler, A., Wieczorek, D., Gross, O., Ermisch-Omran, B., Werberger, A., Skalej, M., Janecke, A.R., Soliman, N.A., Mane, S.M., Lifton, R.P., Kadlec, J., Guccione, E., Schmeisser, M.J., Zenker, M. and Hildebrandt, F. Mutations in PRDM15 are a novel cause of galloway-mowat syndrome.
J. Am. Soc. Nephrol. 32: 580-596 (2021).

Kumar, R., Oliver, C., Brun, C., Juarez-Martinez, A.B., Tarabay, Y., Kadlec, J. and de Massy B. Mouse REC114 is essential for meiotic DNA double-strand break formation and forms a complex with MEI4. Life Sci. Alliance, 1:e201800259. (2018)

Diagouraga, B., Clément, J.A.J., Duret, L., Kadlec, J., de Massy, B. and Baudat, F. PRDM9 Methyltransferase Activity Is Essential for Meiotic DNA Double-Strand Break Formation at Its Binding Sites. Mol. Cell, 69:853-865 (2018)

Touat-Todeschini, L., Shichino, Y., Dangin, M., Thierry-Mieg, N., Gilquin, B., Hiriart, E., Sachidanandam, R., Lambert, E., Brettschneider, J., Reuter, M., Kadlec, J., Pillai, R., Yamashita, A., Yamamoto, M., and Verdel. A. Selective termination of lncRNA transcription promotes heterochromatin silencing and cell differentiation. EMBO J. 36:2626-2641. (2017)

El Omari, K., Iourin, O., Kadlec, J., Harlos, K., Sutton, G., Grimes, J.M., and Stuart, D.I. Unexpected structure for the N-terminal domain of Hepatitis C virus envelope glycoprotein E1. Nat. Commun. 5: 4874 (2014).

El Omari, K., Iourin, O., Kadlec,J., Fearn, R., Hall, D.R., Harlos, K., Grimes, J.M., and Stuart, D.I. Pushing the limits of Sulfur-SAD phasing, de novo structure solution of the N-terminal domain of the ectodomain of HCV E1. Acta Crystallogr. D Biol. Crystallogr. 70:2197-2203 (2014)

Xiol, J., Spinelli, P., Laussmann, M.A., Homolka, D., Yang, Z., Cora, E., Couté, Y., Conn, S., Kadlec, J., Sachidanandam, R., Kaksonen, M., Cusack, S., Ephrussi A., and Pillai, R.S. RNA clamping by Vasa assembles a piRNA Amplifier complex on transposon transcripts.
Cell, 157:1698-711 (2014)

Dias, J., Nguyen, N., Georgiev, P., Gaub, A., Brettschneider, J., Cusack, S., Kadlec, J.* and Akhtar, A.* Structural analysis of the KANSL1/WDR5/KANSL2 complex reveals that WDR5 is required for efficient assembly and chromatin targeting of the NSL complex.
Genes Dev. 28: 929-942 (2014)

Guilligay, D., Kadlec, J., Crepin, T., Lunardi,T., Bouvier, D., Kochs, G., Ruigrok, R. and Cusack, S., Comparative structural and functional analysis of orthomyxovirus polymerase cap-snatching domains. PLOS One 9:e84973 (2014)

Wu, H., Mathioudakis, N., Diagouraga, B., Dong A., Dombrovski, L., Baudat. F., Cusack, S., de Massy, B.* and Kadlec, J.* Molecular basis for the regulation of the H3K4 methyltransferase activity of PRDM9. Cell Rep. 5:13-20 (2013)

Najmanova, L., Kutejova, E., Kadlec, J., Polan, M., Olsovska, J., Benada, O., Novotna, J., Kamenik, Z., Halada, P., Bauer, J., and Janata., J Characterization of N-demethyllincosamide methyltransferases LmbJ and CcbJ. ChemBioChem 14:2259-62 (2013)

Iourin, O., Harlos, K., El Omari, K., Lu, W., Kadlec, J., Iqbal, M., Meier, C., Palmer A., Jones, I., Thomas, C., Brownlie, J., Grimes, J.M., and Stuart, D.I Expression, purification and crystallization of the ectodomain of the envelope glycoprotein E2 from Bovine viral diarrhoea virus. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 69:35-38 (2013)

Hallacli, E., Lipp, M., Georgiev, P., Spielman, C., Cusack, S., Akhtar, A.* and Kadlec, J.* MSL1-mediated dimerization of the dosage compensation complex is essential for male X-chromosome regulation in Drosophila. Mol. Cell 48:587-600 (2012)

O’Flynn, N.M.J., Patel, A., Kadlec, J. and Jones I.M. Improving promiscuous mammalian cell entry by the baculovirus AcMNPV. Biosci. Rep. 33:23-36 (2012)

Mathioudakis, N., Palencia, A., Kadlec, J., Round, A., Tripsianes, K., Sattler, M., Pillai, R.S. and Cusack, S. The multiple Tudor domain-containing protein TDRD1 is a molecular scaffold for mouse Piwi proteins and piRNA biogenesis factors. RNA 18:2056-72 (2012)

Kadlec, J., Hallacli, E., Lipp, M., Holz, H., Sanchez-Weatherby, J., Cusack, S.* and Akhtar, A.* Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1. Nat. Struct. Mol. Biol. 18:142-149 (2011)

Raja, S.J., Charapitsa, I., Conrad, T., Vaquerizas, J.M., Gebhardt, P., Holz, H., Kadlec, J., Fraterman, S., Luscombe, N.M. and Akhtar, A. The nonspecific lethal complex is a transcriptional regulator in Drosophila. Mol. Cell 38:827-41 (2010)

Sanchez-Weatherby, J., Bowler, M.W., Huet, J., Gobbo, A., Felisaz, F., Lavault, B., Moya, R., Kadlec, J., Ravelli, R.B. and Cipriani, F. Improving diffraction by humidity control: a novel device compatible with X-ray beamlines. Acta Crystallogr. D Biol. Crystallogr. 65:1237-46. (2009)

Clerici M., Mourão, A., Gutsche, I., Gehring, N.H, Hentze, M., Kulozik A., Kadlec J., Sattler M., and Cusack S. Unusual bipartite mode of interaction between the nonsense mediated decay factors UPF1 and UPF2. EMBO J. 28:2293-2306 (2009).

Kadlec, J., Loureiro, S., Abrescia, N.G.A., Stuart, D.I. and Jones, I.M. The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines.
Nat. Struct. Mol. Biol. 15: 1024-30 (2008)

Walter, T.S. Mancini, E.J., Kadlec, J., Grahem, S.C., Assenberg, R., Ren, J., Sainsbury, S., Owens, R.J., Stuart, D.I., Grimes, J.M. and Harlos, K. Semi-automated microseeding of nanolitre crystallization experiments. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64, 14-8 (2008)

Kadlec, J., Guilligay, D., Ravelli, R.B. and Cusack, S. Crystal structure of the UPF2-interacting domain of nonsense-mediated mRNA decay factor UPF1. RNA 12, 1817–1824 (2006)

Kadlec, J., Izaurralde, E. and Cusack, S. The structural basis for the interaction between nonsense-mediated mRNA decay factors UPF2 and UPF3.
Nat. Struct. Mol. Biol. 11, 330-337 (2004)

Bracher, A., Kadlec, J., Betz, H. and Weissenhorn, W. X-ray structure of a neuronal complexin-SNARE complex from squid.
J. Biol. Chem. 277, 26517-26523 (2002)