Publications

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* → equal contribution
# →
corresponding author
bold Jonas group members

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2024

Sabath K*, Qiu C*, Jonas S#. Assembly mechanism of Integrator’s RNA cleavage module. 84, 2882-2899.e10 (2024) Mol. Cell external page doi: 10.1016/j.molcel.2024.06.032

Karasu ME, Jahnke L, Joseph BJ, Amerzhanova Y, Mironov A, Shu X, Schröder MS, Gvozdenovic A, Sala I, Zavolan M, Jonas S, Corn JE#.
CCAR1 promotes DNA repair via alternative splicing. 84, 2634-2647.e9 (2024) Mol. Cell external page doi: 10.1016/j.molcel.2024.06.011; preprint bioRxiv external page doi: 10.1101/2023.09.18.557780

Sabath K*, Nabih A*, Arnold C, Moussa R, Domjan D, Zaugg JB, Jonas S#. Basis of gene-specific transcription regulation by the Integrator complex. 84, 2525-2541.e12 (2024) Mol. Cell external page doi: 10.1016/j.molcel.2024.05.027; preprint bioRxiv external page doi: 10.1101/2024.01.24.576984

2023

Beusch I, Rao B, Studer M, Luhovska T, Šukytė V, Lei S, Oses-Prieto JA, SeGraves E, Burlingame A, Jonas S, Madhani HD#. Targeted high-throughput mutagenesis of the human spliceosome reveals its in vivo operating principles. 83, 2387-2389 (2023) Mol. Cell external page doi: 10.1016/j.molcel.2023.06.003; preprint bioRxiv external page doi: 10.1101/2022.11.13.516350

2022

Sabath K, Jonas S#. Take a break: Transcription regulation and RNA processing by the Integrator complex. 77 (2022) Curr. Opin. Struct. Biol. external page doi: 10.1016/j.sbi.2022.102443

de Vries T*, Martelly W*, Campagne S*, Sabath K, Sarnowski CP, Wong J, Leitner A, Jonas S#, Sharma S#, Allain FHT#. Sequence-specific RNA recognition by an RGG motif connects U1 and U2 snRNP for spliceosome assembly. 119, e2114092119 (2022) Proc. Natl. Acad. Sci. USA. external page doi: 10.1073/pnas.2114092119

2021

Callon M*, Malär AA*, Pfister S*, Římal V*, Weber ME*, Wiegand T*, Zehnder J*, Chávez M, Cadalbert R, Deb R, Däpp A, Fogeron ML, Hunkeler A, Lecoq L, Torosyan A, Zyla D, Glockshuber R, Jonas S, Nassal M, Ernst M#, Böckmann A#, Meier BH#. Biomolecular solid-state NMR spectroscopy at 1200 MHz: the gain in resolution. 75, 255–272 (2021) J. Biomol. NMR. external page doi: 10.1007/s10858-021-00373-x

Bohnsack KE, Ficner R, Bohnsack MT#, Jonas S#. Regulation of DEAH-box RNA helicases by G-patch proteins. 402, 255-272 (2021) Biol. Chem. external page doi: 10.1515/hsz-2020-0338

2020

Sabath K, Stäubli ML, Leitner A, Moes M, Jonas S#. INTS10–INTS13–INTS14 form a functional module of Integrator that binds nucleic acids and the cleavage module. 11, 3422 (2020) Nat. Commun. external page doi: 10.1038/s41467-020-17232-2

Studer MK, Ivanović L, Weber ME, Marti S, Jonas S#. Structural basis for DEAH-helicase activation by G-patch proteins. 117, 7159–7170 (2020) Proc. Natl. Acad. Sci. USA. external page doi: 10.1073/pnas.1913880117

Montellese C, van den Heuvel J, Ashiono C, Dörner K, Melnik A, Jonas S, Zemp I, Picotti P, Gillet LC, Kutay U#. USP16 counteracts mono-ubiquitination of RPS27a and promotes maturation of the 40S ribosomal subunit. 9, pii: e54435 (2020) Elife.  external page doi: 10.7554/eLife.54435

2019

van Loo B, Bayer CD, Fischer G, Jonas S, Valkov E, Mohamed MF, Vorobieva A, Dutruel C, Hyvönen M#, Hollfelder F#. Balancing specificity and promiscuity in enzyme evolution: Multidimensional activity transitions in the alkaline phosphatase superfamily. 141, 370–387 (2019) J. Am. Chem. Soc. external page doi: 10.1021/jacs.8b10290

2018

Miton CM, Jonas S, Fischer G, Duarte F, Mohamed MF, van Loo B, Kintses B, Kamerlin SCL, Tokuriki N, Hyvönen M, Hollfelder F#. Evolutionary repurposing of a sulfatase: A new Michaelis complex leads to efficient transition state charge offset. 115, E7293–E7302 (2018) Proc. Natl. Acad. Sci. USA. external page doi: 10.1073/pnas.1607817115

2017

Valkov E, Jonas S#, Weichenrieder O#. Mille viae in eukaryotic mRNA decapping. 47, 40–51 (2017) Curr. Opin. Struct. Biol. external page doi: 10.1016/j.sbi.2017.05.009

2016

Bammert L, Jonas S, Ungricht R, Kutay U#. Human AATF/Che-1 forms a nucleolar protein complex with NGDN and NOL10 required for 40S ribosomal subunit synthesis. 44, 9803–9820 (2016) Nucleic Acids Res. external page doi: 10.1093/nar/gkw790

Valkov E*, Muthukumar S*, Chang CT*, Jonas S#, Weichenrieder O#, Izaurralde E#. Structure of the Dcp2-Dcp1 mRNA-decapping complex in the activated conformation. 23, 574–579 (2016) Nat. Struct. Mol. Biol. external page doi: 10.1038/nsmb.3232

2015

Jonas S, Izaurralde E#. Towards a molecular understanding of microRNA-mediated gene silencing. 16, 421–433 (2015) Nat. Rev. Genet. external page doi: 10.1038/nrg3965

2014

Jonas S*, Christie M*, Peter D, Bhandari D, Loh B, Huntzinger E, Weichenrieder O#, Izaurralde E#. An asymmetric PAN3 dimer recruits a single PAN2 exonuclease to mediate mRNA deadenylation and decay. 21, 599–608 (2014) Nat. Struct. Mol. Biol. external page doi: 10.1038/nsmb.2837
highlighted: external page "News and Views" in NSMB and external page "Have you seen?"  in EMBO J.

Bhandari D*, Raisch T*, Weichenrieder O, Jonas S#, Izaurralde E#. Structural basis for the Nanos-mediated recruitment of the CCR4-NOT complex and translational repression. 28, 888–901 (2014) Genes Dev. external page doi: 10.1101/gad.237289.113
recommended: external page Faculty of 1000

Chang CT, Bercovich N, Loh B, Jonas S, Izaurralde E#. The activation of the decapping enzyme DCP2 by DCP1 occurs on the EDC4 scaffold and involves a conserved loop in DCP1. 42, 5217–5233 (2014) Nucleic Acids Res. external page doi: 10.1093/nar/gku129

2013

Jonas S, Izaurralde E#. The role of disordered protein regions in the assembly of decapping complexes and RNP granules. 27, 2628–2641 (2013) Genes Dev. external page doi: 10.1101/gad.227843.113

Schneider AM, Schmidt S, Jonas S, Vollmer B, Khazina E, Weichenrieder O#. Structure and properties of the esterase from non-LTR retrotransposons suggest a role for lipids in retrotransposition. 41, 10563–10572 (2013) Nucleic Acids Res. external page doi:10.1093/nar/gkt786

Boland A*, Chen Y*, Raisch T*, Jonas S*, Kuzuoğlu-Öztürk D, Wohlbold L, Weichenrieder O#, Izaurralde E#. Structure and assembly of the NOT module of the human CCR4-NOT complex. 20, 1289–1297 (2013) Nat. Struct. Mol. Biol. external page doi: 10.1038/nsmb.2681

Loh B, Jonas S, Izaurralde E#. The SMG5-SMG7 heterodimer directly recruits the CCR4-NOT deadenylase complex to mRNAs containing nonsense codons via interaction with POP2. 27, 2125–2138 (2013) Genes Dev. external page doi: 10.1101/gad.226951.113

Jonas S, Weichenrieder O, Izaurralde E#. An unusual arrangement of two 14-3-3-like domains in the SMG5-SMG7 heterodimer is required for efficient nonsense-mediated mRNA decay. 27, 211–225 (2013) Genes Dev. external page doi: 10.1101/gad.206672.112

2010

Kashima I, Jonas S, Jayachandran U, Buchwald G, Conti E, Lupas AN, Izaurralde E#. SMG6 interacts with the exon junction complex via two conserved EJC-binding motifs (EBMs) required for nonsense-mediated mRNA decay. 24, 2440–2450 (2010) Genes Dev. external page doi:10.1101/gad.604610

van Loo B*, Jonas S*, Babtie AC, Benjdia A, Berteau O, Hyvönen M, Hollfelder F#. An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily. 107, 2740–2745 (2010) Proc. Natl. Acad. Sci. USA. external page doi:10.1073/pnas.0903951107

2009

Jonas S, Hollfelder F#. Mapping catalytic promiscuity in the alkaline phosphatase superfamily. 81, 731–742 (2009) Pure Appl. Chem. external page doi:10.1351/PAC-CON-08-10-20

2008

Jonas S, Hollfelder F#. Mechanism and catalytic promiscuity: Emerging mechanistic principles for identification and manipulation of catalytically promiscuous enzymes. U. Bornscheuer and S. Lutz (eds.), Wiley VCH, 47–79 (2008) Handbook of Protein Engineering. external page doi: 10.1002/9783527634026.ch3

Jonas S, van Loo B, Hyvönen M#, Hollfelder F#. A new member of the alkaline phosphatase superfamily with a formylglycine nucleophile: structural and kinetic characterisation of a phosphonate monoester hydrolase/phosphodiesterase from Rhizobium leguminosarum. 384, 120–136 (2008) J. Mol. Biol. external page doi:10.1016/j.jmb.2008.08.072

2005

Karbstein K, Jonas S, Doudna JA#. An essential GTPase promotes assembly of pre-ribosomal RNA processing complexes. 20, 633–643 (2005) Mol. Cell. external page doi: 10.1016/j.molcel.2005.09.017
highlighted: external page "Preview" in Mol. Cell

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