Publications
- Krause L., Chakraborty, A.; Andreou, A.; Klostermeier, D. Linking translation factor conformational dynamics with translation efficiencies and gene expression . In: Biophysical Journal 121 (), №. - 3, pp. 338a–339a. doi: .
- Klostermeier, D. Analysis of the conformational space and dynamics of RNA helicases by single-molecule FRET in solution and on surfaces . In: Methods in Enzymology 673 (), pp. 251–310. doi: 10.1016/bs.mie.2022.03.043.
- Krause, L.; Willing, F.; Andreou, A.; Klostermeier, D. The domains of yeast eIF4G, eIF4E and the cap fine-tune eIF4A activities through an intricate network of stimulatory and inhibitory effects . In: Nucleic Acids Research 50 (), №. - 11, pp. 6497–6510. doi: 10.1093/nar/gkac437.
- Chakraborty, A.; Krause, L.; Klostermeier, D. Determination of rate constants for conformational changes of RNA helicases by single-molecule FRET TIRF microscopy . In: Methods 204 (), pp. 428–441. doi: 10.1016/j.ymeth.2022.03.004.
- Hirsch, J., Klostermeier, D. What makes a type IIA topoisomerase a gyrase or a Topo IV? . In: Nucleic Acids Res . 2021 (). doi: 10.1093/nar/gkab270.
- Klostermeier D. Towards Conformation-Sensitive Inhibition of Gyrase: Implications of Mechanistic Insight for the Identification and Improvement of Inhibitors . In: Molecules . 26 (), №. - 5. doi: 10.3390/molecules26051234..
- Donsbach P, Klostermeier D. Regulation of RNA helicase activity: principles and examples . In: Biol Chem . 2021 (). doi: 10.1515/hsz-2020-0362.
- Krause L, Klostermeier D. Probing RNA Helicase Conformational Changes by Single-Molecule FRET Microscopy . In: Methods Mol Biol 2209 (), pp. 119–132. doi: 10.1007/978-1-0716-0935-4_8.
- Klostermeier, D. Highlight: RNA helicases–structure, function, mechanism and regulation . In: Biological Chemistry Hoppe-Seyler 402 (), №. - 5, pp. 527–528. doi: 10.1515/hsz-2021-0194.
- Romanovska, A. ;Keil, J.; Tophoven, J.; Furkan Oruc, M.; Schmidt, M.; Breisch, M.; Sengstock*, C.; Weidlich, D.Klostermeier* D., Tiller* J. Conjugates of ciprofloxacin and amphiphilic block copoly (2-alkyl-2-oxazolines) s overcome efflux pumps and are active against CIP-resistant bacteria . In: Molecular pharmaceutics 18 (), №. - 9, pp. 3532–3543. doi: 10.1021/acs.molpharmaceut.1c00430.
- Donsbach P, Yee BA, Sanchez-Hevia D, Berenguer J, Aigner S, Yeo GW, Klostermeier D. The Thermus thermophilus DEAD-box protein Hera is a general RNA binding protein and plays a key role in tRNA metabolism . In: RNA . 11 (), pp. 1557–1574. doi: 10.1261/rna.075580.120.
- Collin F, Weisslocker-Schaetzel M, Klostermeier D. A β-hairpin is a Minimal Latch that Supports Positive Supercoiling by Reverse Gyrase . In: J Mol Biol 432 (), №. - 16, pp. 4762–4771. doi: 10.1016/j.jmb.2020.06.018.
- Leemans M, Galicia C, Deyaert E, Daems E, Krause L, Paesmans J, Pardon E, Steyaert J, Kortholt A, Sobott F, Klostermeier D, Versées W. Allosteric modulation of the GTPase activity of a bacterial LRRK2 homolog by conformation-specific Nanobodies . In: Biochem J . 477 (), №. - 7, pp. 1203–1218. doi: 10.1042/BCJ20190843.
- Weidlich D, Klostermeier D. Functional interactions between gyrase subunits are optimized in a species-specific manner . In: J Biol Chem . 295 (), №. - 8, pp. 2299–2312. doi: 10.1074/jbc.RA119.010245.
- Stelljes, J., Weidlich, D., Gubaev, A., Klostermeier, D. Gyrase containing a single C-terminal domain catalyzes negative supercoiling of DNA by decreasing the linking number in steps of two . In: Nucleic Acids Research 46 (), №. - 13, pp. 6773–6784. doi: 10.1093/nar/gky470.
- Klostermeier, Dagmar Why Two? On the Role of (A-)Symmetry in Negative Supercoiling of DNA by Gyrase . In: Int. J. Mol. Sci. 19 (). doi: 10.3390/ijms19051489.
- Hartmann, S., Gubaev, A., Klostermeier, D. Binding and hydrolysis of a single ATP is sufficient for negative supercoiling of DNA by gyrase . In: J. Mol. Biol. 429 (), №. - 23, pp. 3717–3729. doi: 10.1016/j.jmb.2017.10.005.
- Samantanga, B., Andreou, A.Z., Klostermeier, D. Allosteric regulation of helicase core activities of the DEAD-box helicase YxiN by RNA binding to its RNA recognitation motif . In: Nuc. Acids Res. 45 (), №. - 4, pp. 1994–2006. doi: 10.1093/nar/gkx014.
- Klostermeier, D., Rudolph, M.G. Biophysical Chemistry. 0th Ed. N/A: unbekannt / n.a. / unknown. , . ISBN 9781482252231. doi: .
- Andreou, A., Harms, U., Klostermeier, D. eIF4B stimulates eIF4A ATPase and unwinding activities by direct interaction through its 7-repeats region . In: RNA Biol. 14 (), №. - 1, pp. 113–123. doi: 10.1080/15476286.2016.1259782.
- Hartmann, S., Weidlich, D., Klostermeier, D. Single-Molecule Confocal FRET Microscopy to Dissect Conformational Changes in the Catalytic Cycle of DNA Topoisomerases . In: Methods Enzymol 581 (), pp. 317–351. doi: 10.1016/bs.mie.2016.08.013.
- Gubaev, A., Weidlich, D., Klostermeier, D. DNA gyrase with a single catalytic tyrosine can catalyze DNA supercoiling by a nicking-closing mechanism . In: Nucl. Acids Res. 44 (), №. - 21, pp. 10354–10366. doi: 10.1093/nar/gkw740.
- Heininger, A.U., Hackert, P., Andreou, A.Z., Boon, K.L., Memet, I., Prior, M., Clancy, A., Schmidt, B., Urlaub, H., Schleiff, E., Sloan, K.E., Deckers, M., Lührmann, R., Enderlein, J., Klostermeier, D., Rehling, P., Bohnsack, M.T. Protein cofactor competition regulates the action of a multifunctional RNA helicase in different pathways . In: RNA Biol 13 (), №. - 3, pp. 320–330. doi: 10.1080/15476286.2016.1142038.
- Rudolph, M.G., Klostermeier, D. When core competence is not enough: functional interplay of the DEAD-box helicase core with ancillary domains and auxilliary factors in RNA binding and unwinding . In: Biol. Chem. 396 (), №. - 8, pp. 849–865. doi: 10.1515/hsz-2014-0277.
- Nianios, D., Thierbach, S., Steimer, L., Lulchev, P., Klostermeier, D., Fetzner, S. Nickel quercetinase, a "promiscuous metalloenzyme: metal incorporation and metal ligand substitution studies . In: BMC Biochem 16 (), №. - 10. doi: 10.1186/s12858-015-0039-4.
- Samatanga, B., Klostermeier, D. DEAD-box RNA helicase domains exhibit a continuum between complete functional independence and high thermodynamic coupling in nucleotide and RNA duplex recognition . In: Nucl. Acids Res 42 (), №. - 16, pp. 10644–10654. doi: .
- Del Toro Duany, Y., Ganguly, A., Klostermeier, D. Differential contributions of the latch in Thermotoga maritima reverse gyrase to binding of single-stranded DNA before and after ATP hydrolysis . In: Biol. Chem. 395 (), №. - 1, pp. 83–93. doi: 10.1515/hsz-2013-0177.
- Andreou, A.Z., Klostermeier, D. eIF4B and eIF4G jointly stimulate eIF4A ATPase and unwinding activities by modulation of the eIF4A conformational cycle . In: J. Mol. Biol. 426 (), №. - 1, pp. 51–61. doi: 10.1016/j.jmb.2013.09.027.
- Lanz, M.A., Farhat, M., Klostermeier, D. The acidic C-terminal tail of the GyrA subunit moderates the DNA supercoiling activity of Bacillus subtilis gyrase . In: J. Biol. Chem. 289 (), №. - 18, pp. 12275–12285. doi: 10.1074/jbc.M114.547745.
- Gubaev, A., Klostermeier, D. The mechanism of negative DNA supercoiling: a cascade of DNA-induced conformational changes prepares gyrase for strand passage . In: DNA Repair 16 (), pp. 23–24. doi: 10.1016/j.dnarep.2014.01.011.
- Harms, U., Andreou, A.Z., Gubaev, A., Klostermeier, D. eIF4B, eIF4G and RNA regulate eIF4A activity in translation initiation by modulating the eIF4A conformational cycle . In: Nucl. Acids Res. 42 (), №. - 12, pp. 7911–7922. doi: 10.1093/nar/gku440.
- Lulchev, P., Klostermeier, D. Reverse gyrase-recent advances and current mechanistic understanding of positive DNA supercoiling . In: Nucl. Acids Res. 42 (), pp. 8200–8213. doi: 10.1093/nar/gku589.
- Andreou, A.Z., Klostermeier, D. Fluorescence Methods in the Investigation of the DEAD-Box Helicase Mechanism . In: Experienta Supplementum 105 (), pp. 161–192. doi: 10.1007/978-3-0348-0856-9_8.
- Klostermeier, D. Rearranging RNA structures at 75°C? Towards the physiologic function of the DEAD-box helicase Hera from Thermus thermophilus”, for the Biopolymers Special Issue “Nucleic acids . In: Biopolymers 99 (), №. - 12, pp. 1137–1146. doi: 10.1002/bip.22316.
- Gubaev, A., Klostermeier, D. Single molecule FRET reveals DNA- and nucleotide-induced conformational changes in DNA gyrase preceding the strand passage reaction, for the DNA repair Special Issue “Single molecule approaches: watching DNA repair one molecule at a time . In: DNA repair (). doi: 10.1042/BST0390611.
- Del Toro Duany, Y., Ganguly, A., Klostermeier, D. Differential contributions of the latch in Thermotoga maritima reverse gyrase to binding of single-stranded DNA before and after ATP hydrolysis . In: Biol. Chem. 394 (). doi: 10.1515/hsz-2013-0177. [online first]
- Andreou, A. Z., Klostermeier, D. eIF4B and eIF4G jointly stimulate eIF4A ATPase and unwinding activities by modulation of the eIF4A conformational cycle . In: J. Mol. Biol. 2013 (). doi: 10.1016/j.jmb.2013.09.027.. [online first]
- Steimer, L.; Wurm, J.P.; Linden, M.H.; Rudolph, M.G.; Wöhnert, J.; Klostermeier, D. Recognition of two distinct elements in the RNA substrate by the RNA-binding domain of the T. thermophilus DEAD box helicase Hera . In: Nucl. Acids Res. 41 (), №. - 12, pp. 6259–6272. doi: 10.1093/nar/gkt323.
- Rudolph, M.G.; Klostermeier, D. Mapping the Spectrum of Conformational States of the DNA- and C-Gates in Bacillus subtilis Gyrase . In: J. Mol. Biol. 2013 (). doi: .
- Klostermeier, D. Lifelong companions: RNA helicases and their roles in RNA metabolism . In: RNA Biol. 10 (), №. - 1, pp. 2–3. doi: .
- Rudolph, M.G.; del Toro Duany, Y.; Jungblut, S.P.; Ganguly, A.; Klostermeier, D. Crystal structures of Thermotoga maritima reverse gyrase: inferences for the mechanism of positive DNA supercoiling . In: Nucl. Acids Res. 41 (), №. - 2, pp. 1058–1070. doi: 10.1093/nar/gks1073.
- Ganguly, A.; del Toro Duany, Y.; Klostermeier, D. Reverse gyrase transiently unwinds double-stranded DNA in an ATP-dependent reaction . In: J. Mol. Biol. 425 (), №. - 1, pp. 32–40. doi: .
- Andreou, A.Z., Klostermeier, D. DEAD-box helicase conformational changes monitored by single molecule fluorescence resonance energy transfer”, in “RNA Helicases: Analysis of Molecular Mechanisms and Biological Functions . In: Methods in Enzymology 511 (), pp. 75–109. doi: .
- Steimer, L., Klostermeier, D. RNA helicases in infection and disease”, Special Issue on “RNA and Disease . In: RNA Biology 9 (), №. - 6, pp. 751–771. doi: .
- Andreou, A.Z., Klostermeier, D. The DEAD box helicase eIF4A: paradigm or special case?” for the RNA Biology Special Issue on “RNA helicases . In: RNA Biology 10 (), №. - 1, pp. 19–32. doi: .
- Andreou, A., Klostermeier, D. Conformational changes of DEAD-box helicases monitored by single molecule fluorescence resonance energy transfer . In: Methods Enzymol. 511 (), pp. 75–109. doi: .
- Lanz, M., Klostermeier, D. The GyrA-box determines the geometry of DNA bound to gyrase and couples DNA binding to the nucleotide cycle . In: Nucleic Acids Res. 40 (), №. - 21, pp. 10893–10903. doi: .
- Andreou, A., Klostermeier, D. The DEAD-box helicase elF4A: Paradigm or the odd one out? . In: RNA Biol. 10 (), №. - 1, pp. 1–14. doi: .
- Ganguly, A., Del Toro Duany, Y., Klostermeier, D. Reverse Gyrase Transiently Unwinds Double-Stranded DNA in an ATP-Dependent Reaction . In: J. Mol. Biol. 425 (), №. - 1, pp. 32–40. doi: .
- Rudolph, MG., Del Toro Duany, Y., Jungblut, SP., Ganguly, A., Klostermeier, D. Crystal structures of Thermotoga maritima reverse gyrase: inferences for the mechanism of positive DNA supercoiling . In: Nucleic Acids Res. 2012 (), pp. 1–13. doi: .
- Gubaev A., Klostermeier, D. Potassium ions are required for nucleotide-induced closure of gyrase N-gate . In: J. Biol. Chem 287 (), №. - 14, pp. 10916–10921. doi: .
- Klostermeier D Highlight: Mechanisms of RNA-mediated regulation . In: Biological Chemistry 392 (), №. - 4, p. 275. doi: 10.1515/BC.2011.047.
- Hammann C, Hartmann RK, Helm M, Klostermeier D, Marchfelder A, Suess B, Vörtler S Regulatory RNAs and beyond . In: EMBO Reports 12 (), №. - 8, pp. 751–753. doi: 10.1038/embor.2011.150.
- Ganguly A, del Toro Duany Y, Rudolph MG, Klostermeier D The latch modulates nucleotide and DNA binding to the helicase-like domain of Thermotoga maritima reverse gyrase and is required for positive DNA supercoiling . In: Nucleic Acids Research 39 (), №. - 5, pp. 1789–1800. doi: 10.1093/nar/gkq1048.
- Strohmeier J., Hertel I., Diederichsen U., Rudolph M.G., Klostermeier D. Changing nucleotide specificity of the DEAD-box helicase Hera abrogates communication between the Q-motif and the P-loop . In: Biological Chemistry 329 (), №. - 4, pp. 357–369. doi: 10.1515/BC.2011.034.
- Klostermeier D Single-molecule FRET reveals nucleotide-driven conformational changes in molecular machines and their link to RNA unwinding and DNA supercoiling . In: Biochemical Society Transactions 39 (), №. - 2, pp. 611–616. doi: 10.1042/BST0390611.
- del Toro Duany Y, Klostermeier D Nucleotide-driven conformational changes in the reverse gyrase helicase-like domain couple the nucleotide cycle to DNA processing . In: Physical Chemistry Chemical Physics (), p. Paper. doi: 10.1039/C0CP02859B.
- Gubaev Ayrat, Klostermeier Dagmar DNA-induced narrowing of the gyrase N-gate coordinates T-segment capture and strand passage. . In: Proceedings of the National Academy of Sciences of the United States of America 108 (), №. - 34, pp. 14085–14090. doi: 10.1073/pnas.1102100108.
- Lanz Martin A, Klostermeier Dagmar Guiding strand passage: DNA-induced movement of the gyrase C-terminal domains defines an early step in the supercoiling cycle.
. In: Nucleic Acids Research (), pp. 1–14. doi: 10.1093/nar/gkr680.
- Del Toro Duany, Y., Klostermeier, D., Rudolph, M.G. The conformational flexibility of the helicase-like domain from Thermotoga maritima reverse gyrase is restricted by the topoisomerase domain . In: Biochemistry 50 (), №. - 26, pp. 5816–5823. doi: .
- Hilbert, M., Kebbel, F., Gubaev, A., Klostermeier, D. eIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanism . In: Nucl. Acids Res. 2011 (), №. - 39(6), pp. 2260–2270. doi: .
- Aregger R, Klostermeier D The DEAD Box Helicase YxiN Maintains a Closed Conformation during ATP Hydrolysis . In: Biochemistry 48 (), №. - 45, pp. 10679–10681. doi: 10.1021/bi901278p.
- Hilbert, M., Karow, A.R., Klostermeier, D. The mechanism of ATP-dependent RNA unwinding by DEAD-box proteins . In: Biological Chemistry 390 (), №. - 12, pp. 1237–1250. doi: 10.1515/BC.2009.135.
- Dagmar Klostermeier, Lidia Guzy, Anja Mihr and Rajah Scheepers (Eds.): Wohin mit uns? – Wissenschaftlerinnen und Wissenschaftler der Zukunft. 0th Ed. Lausanne: Peter Lang. , . ISBN 978-3-631-58114-8. doi: .
- Rudolph M.G. , Klostermeier D The Thermus thermophilus DEAD box helicase Hera contains a modified RNA recognition motif domain loosely connected to the helicase core . In: RNA 15 (), №. - 11, pp. 1993–2001. doi: 10.1261/rna.1820009.
- Karow A.R., Klostermeier D. A conformational change in the helicase core is necessary but not sufficient for RNA unwinding by the DEAD box helicase YxiN . In: Nucleic Acids Research 37 (), №. - 13, pp. 4464–4471. doi: 10.1093/nar/gkp397.
- Rudolph M.G., Wittmann J.G., and Klostermeier D. Crystallization and preliminary characterization of the Thermus thermophilus RNA helicase Hera C-terminal domain . In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications 65 (), №. - 3, pp. 248–252. doi: 10.1107/S1744309108043145.
- Klostermeier D., Rudolph A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility . In: Nucleic Acids Research 37 (), №. - 2, pp. 421–430. doi: 10.1093/nar/gkn947.
- Gubaev A., Hilbert M. , Klostermeier D. The DNA-gate of Bacillus subtilis gyrase is predominantly in the closed conformation during the DNA supercoiling reaction . In: Proceedings of the National Academy of Sciences of the United States of America 106 (), №. - 32, pp. 13278–13283. doi: 10.1073/pnas.0902493106.
- Linden M.L., Hartmann R.K., Klostermeier D. The putative RNase P motif in the DEAD box helicase Hera is dispensable for efficient interaction with RNA and helicase activity . In: Nucleic Acids Research 36 (), №. - 18, pp. 5800–5811. doi: 10.1093/nar/gkn581.
- Del Toro Duany Y., Jungblut S.P., Schmidt A.S., Klostermeier D. The reverse gyrase helicase-like domain is a nucleotide-dependent switch that is attenuated by the topoisomerase domain . In: Nucleic Acids Research 36 (), №. - 18, pp. 5882–5895. doi: 10.1093/nar/gkn587.
- Theissen B., Karow A.R., Köhler J., Gubaev A., Klostermeier D. RNA and ATP cooperatively induce a conformational change in a DEAD box helicase . In: Proceedings of the National Academy of Sciences of the United States of America 105 (), №. - 2, pp. 548–553. doi: 10.1073/pnas.0705488105.
- Jungblut S.P., Klostermeier D. Adenosine 5′-O-(3-thio)triphosphate (ATPγS) Promotes Positive Supercoiling of DNA by T. maritima Reverse Gyrase . In: Journal of Molecular Biology 371 (), №. - 1, pp. 197–209. doi: 10.1016/j.jmb.2007.05.031.
- Göttler T., Klostermeier D. Dissection of the Nucleotide Cycle of B. subtilis DNA Gyrase and its Modulation by DNA . In: Journal of Molecular Biology 367 (), №. - 5, pp. 1392–1404. doi: 10.1016/j.jmb.2007.01.055.
- Karow A., Theissen B., Klostermeier D. Authentic interdomain communication in an RNA helicase reconstituted by expressed protein ligation of two helicase domains . In: The FEBS Journal 274 (), №. - 2, pp. 463–473. doi: 10.1111/j.1742-4658.2006.05593.x.
- Klostermeier, D., Sears, P., Wong, C.-H., Millar, D.P., Williamson, J.R. A three-fluorophore FRET assay for high-throughput screening of small-molecule inhibitors of ribosome assembly . In: Nucleic Acids Research 32 (), №. - 9, pp. 2707–2715. doi: 10.1093/nar/gkh588.
- Dumitru, G. L., Deuerling, E., Groemping, Y., Klostermeier, D., Restle, T., Reinstein, J. DafA cycles between the DnaK chaperone system and translational machinery . In: Journal of Molecular Biology 339 (), №. - 5, pp. 1179–1189. doi: 10.1016/j.jmb.2004.04.052.
- Klostermeier, D., Millar, D.P. Time-resolved fluorescence resonance energy transfer: A versatile tool for the analysis of nucleic acids . In: Biopolymers 61 (), №. - 3, pp. 159–179. doi: 10.1002/bip.10146.
- Ryder, S.P., Oyelere, A.K., Padilla, J., Klostermeier, D., Millar, D.P., Strobel, S.A Investigation of adenosine base ionization in the hairpin ribozyme by nucleotide analog interference mapping . In: RNA 7 (), №. - 10, pp. 1454–1463. doi: .
- Klostermeier, D., Millar, D.P. RNA conformation and folding studied with fluorescence resonance energy transfer . In: Methods 23 (), №. - 3, pp. 240–254. doi: 10.1006/meth.2000.1135.
- Klostermeier, D., Millar, D.P. Tertiary structure stability of the hairpin ribozyme in its natural and minimal forms: Different energetic contributions from a ribose zipper motif . In: Biochemistry 40 (), №. - 37, pp. 11211–11218. doi: 10.1021/bi010773f.
- Brehmer, D., Ruediger, S., Gaessler, C., Klostermeier D., Packschies, L., Reinstein, J., Mayer. M.P., Bukau, B. Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange . In: Nature Structural Biology 8 (), №. - 5, pp. 427–432. doi: 10.1038/87588.
- Grömping, Y., Klostermeier, D., Herrmann, C., Veit, T., Seidel, R., Reinstein, J. Regulation of ATPase and chaperone cycle of DnaK from Thermus thermophilus by the nucleotide exchange factor GrpE . In: Journal of Molecular Biology 305 (), №. - 5, pp. 1173–1183. doi: 10.1006/jmbi.2000.4373.
- Laufen T., Mayer, M.P., Beisel, C., Klostermeier, D., Mogk, A., Reinstein, J., Bukau, B. Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones . In: Proceedings of the National Academy of Sciences of the United States of America 96 (), №. - 10, pp. 5452–5457. doi: 10.1073/pnas.96.10.5452.
- Klostermeier, D., Seidel, R., Reinstein, J. The functional cycle and regulation of the Thermus thermophilus DnaK chaperone system . In: Journal of Molecular Biology 287 (), №. - 3, pp. 511–525. doi: 10.1006/jmbi.1999.2636.
- Klostermeier, D., Bayer, P., Kraft, M., Frank, R.W., Rösch, P. Spectroscopic investigations of HIV-1 trans-activator and related peptides in aqueous solutions . In: Biophysical Chemistry 63 (), №. - 2-3, pp. 87–96. doi: 10.1016/S0301-4622(96)02243-0.