Hashem Lab

Marie Sissler

Publications and PhD direction

1. Sissler, M., Giegé, R. & Florentz, C. (1996) Arginine aminoacylation identity is context-dependent and ensured by alternate recognition sets in the anticodon loop of accepting tRNA transcripts. EMBO J., 15, 5069-5076.

2. Pütz, J., Wientges, J., Sissler, M., Giegé, R., Florentz, C. & Schwienhorst, A. (1997) Rapid selection of aminoacyl-tRNAs based on biotinylation of a-NH2 group of charged amino acids. Nucleic Acids Res. 25, 1862-1863.

3. Becker, H.F., Motorin, Y., Sissler, M., Florentz, C. & Grosjean, H. (1997) Major identity determinants for enzymatic formation of ribothymidine and pseudouridine in the TY-loop of yeast tRNAs. J. Mol. Biol. 274, 505-518.

4. Sissler, M., Eriani, G., Martin, F., Giegé, R. & Florentz, C. (1997) Mirror image alternative interaction patterns of a same tRNA with either class I arginyl-tRNA synthetase or class II aspartyl-tRNA synthetase. Nucleic Acids Res. 25, 4899-4906.

5. Sissler, M., Giegé, R. & Florentz, C. (1998) The RNA sequence context defines the mechanistic routes by which yeast arginyl-tRNA synthetase charges tRNA. RNA 4, 647-657.

6. Giegé, R., Sissler, M. & Florentz, C. (1998) Universal rules and idiosyncratic features in tRNA identity. Nucleic Acids Res., 26, 5017-5035.

7. Sissler, M., Delorme, C., Bond, J., Renault, P., Ehrlich, S.D. & Francklyn, C. (1999) An aminoacyl-tRNA synthetase paralog with a catalytic role in histidine biosynthesis. Proc. Natl. Acad. Sci. U.S.A., 96, 8985-8990.

8. Florentz, C. & Sissler, M. (2001) Disease-related versus polymorphic mutations in human mitochondrial tRNAs : where is the difference ? EMBO Reports, 2, 481-486.

9. Florentz, C., Pütz, J., Sissler, M. & Giegé, R. (2001) ARNt mitochondriaux humains. Annales de l’Institut Pasteur. Editions scientifiques et médicales Elsevier SAS. 71-86.

10. Florentz, C. & Sissler, M. (2003) “Mitochondrial tRNA aminoacylation and human diseases.” Translation Mechanisms. Landes Bioscience, Georgetown Tx (J. Lapointe & L. Brakier-Gingras Eds), pp129-143.

11. Florentz, C., Sohm, B., Tryoen-Tóth, P., Pütz, J & Sissler, M. (2003) Human mitochondrial tRNAs in health and disease. Cell. Mol. Life Sci. 60, 1356-1375.

12. Fender, A., Sissler, M., Florentz, C. & Giegé, R. (2004) Functional idiosyncrasies of tRNA isoacceptors in cognate and noncognate aminoacylation systems. Biochimie. 86, 21-29.

13. Sissler, M., Helm, M., Frugier M., Giegé, R. & Florentz, C. (2004) Aminoacylation properties of pathology-related human mitochondrial tRNALys variants. RNA. 10, 841-853.

14. Sohm, B., Sissler, M., Park, H., King, M.P. & Florentz, C. (2004) Recognition of human mitochondrial tRNALeu(UUR) by cognate leucyl-tRNA synthetase. J. Mol. Biol. 339,17-29.

15. Fender, A., Geslain, R., Eriani, G., Giegé, R., Sissler, M. & Florentz, C. (2004) A yeast arginine specific tRNA is a remnant aspartate acceptor. Nucleic Acids Res. 32, 5076-5086.

16. Sissler, M., Pütz, J., Fasiolo, F., & Florentz, C. (2005) “Mitochondrial aminoacyl-tRNA synthetases.” The aminoacyl-tRNA synthetases. Landes Bioscience, Georgetown Tx (M. Ibba, S. Cusak & C. Francklyn Eds), chapitre 28.

17. Bonnefond, L., Fender, A., Rudinger-Thirion, J., Giegé, R., Florentz, C. & Sissler, M. (2005). Towards the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS. Biochemistry, 44, 4805-4816.

18.  Champagne, K., Sissler, M., Larabee, Y., Doublié, S. & Francklyn, C. (2005). Activation of the hetero-octameric ATP phosphoribosyl transferase through subunit interface rearrangement by a tRNA synthetase paralog. J. Biol. Chem., 280, 34096-34104.

19. Fender, A., Sauter, C., Messmer, M., Pütz, J., Giegé, R., Florentz, C. & Sissler, M. (2006). Loss of a primordial identity element for a mammalian mitochondrial aminoacylation system. J. Biol. Chem., 281, 15980-15986.

20. Scheper, G.C., van de Klok, T., van Andel, R., van Berkel, C.G.M., Sissler, M., Smet, J., Muravina, T.I., Serkov, S.V., Uziel, G., Bugiani, M., Schiffmann, R., Krägeloh-Mann, I., Smeitink, J., Florentz, C., Van Coster, R., Pronk, J.C., van der Knaap, M.S. (2007) Mitochondrial Aspartyl-tRNA synthetase deficiency causes leukoencephalopathy with brain stem and spinal cord involvement and lactate elevation. Nature Genetics, 39, 534-539.

21. Pütz, J., Dupuis, B., Sissler, M. & Florentz, C. (2007) Mamit-tRNA, a database of mammalian mitochondrial tRNA primary and secondary structures. RNA, 13, 1184-1190.

22. Sissler, M., Lorber, B., Messmer, M., Schaller, A., Pütz, J. & Florentz, C. (2008) Handling mammalian mitochondrial tRNAs and aminoacyl-tRNA synthetases for functional and structural characterization. Methods (Special issue on « Aminoacyl-tRNA synthesis »), 44, 176-189.

32. Schwenzer H., Zoll, J., Florentz C. & Sissler, M. (2014) Pathogenic implications of human mitochondrial aminoacyl-tRNA synthetases. In “Current Chemistry – Aminoacyl-tRNA synthetases: Applications in Chemistry, Biology and Medicine”. Edited by Sunghoon Kim (Seoul, Korea) Springer Editions. Top Curr Chem. 344, 247-292

31. Florentz, C., Pütz, J., Jühling, F., Schwenzer, H., Stadler, P., Lorber, B., Sauter, C. and Sissler, M. (2013). Translation in mammalian mitochondria: Order and disorder linked to tRNAs and aminoacyl-tRNA synthetases. In “Translation in mitochondria and other organelles”. Edited by Anne-Marie Duchêne (Strasbourg, France) Springer Editions. pp55-84.

30. Neuenfeldt, A., Lorber, B., Ennifar, E., Gaudry, A., Sauter, C., Sissler, M. & Florentz, C. (2013) Thermodynamic properties distinguish human mitochondrial aspartyl-tRNA synthetase from bacterial homolog with same 3D architecture. Nucleic Acids Research. 41, 2698-2708.

29. van Berge, L., Kevenaar, J., Polder, E., Gaudry, A., Florentz, C., Sissler, M., van der Knaap, M.S. & Scheper, G.C. (2013) Pathogenic mutations causing LBSL affect mitochondrial aspartyl-tRNA synthetase in diverse ways. Biochemical Journal 450, 345-350.

28. Gaudry, A., Lorber, B., Neuenfeldt, A., Sauter, C., Florentz, C. & Sissler, M. (2012) Redesigned N-terminus enhances expression, solubility, and crystallizability of mitochondrial protein. Protein Engineering, Design and Selection, 25, 473-481.

27. Fender, A., Gaudry, A., Jühling, F., Sissler, M. & Florentz, C. (2012) Adaptation of aminoacylation identity rules to mammalian mitochondria. Biochimie, 94, 1090-1097.

26. Messmer, M., Florentz, C., Schwenzer, H., Scheper, G.C., Van der Knaap, M.S., Maréchal-Drouard, L., & Sissler, M. (2011) A human pathology-related mutation prevents import of an aminoacyl-tRNA synthetase into mitochondria. Biochemical J. (Disease), 433, 441-446.

25. Messmer, M., Pütz, J., Suzuki, T., Suzuki, T., Sauter, C., Sissler, M., & Florentz, C. (2009) Tertiary network in mammalian mitochondrial tRNAAsp revealed by solution probing and phylogeny. NAR, 37, 6881-6895.

24. Messmer, M., Gaudry, A., Sissler, M., & Florentz, C. (2009) Pathology-related mutation A7526G (A9G) helps understanding the 3D structural core of human mitochondrial tRNAAsp. RNA, 15, 1462-1468.

23. Messmer, M., Blais, S. P., Balg, C., Chênevert, R., Grenier, L., Lagüe, P., Sauter, C., Sissler, M., Giegé, R., Lapointe, J. & Florentz, C. (2009) Peculiar inhibition of human mitochondrial aspartyl-tRNA synthetase by adenylate analogs. Biochimie, 91, 596-603.

33. Schwenzer, H., Scheper, G.C., Zorn, N., Moulinier, L., Gaudry, A., Leize, E., Martin, F., Florentz, C., Poch, O. and Sissler, M. (2014). Released selective pressure on a structural domain gives new insights on the functional relaxation of mitochondrial aspartyl-tRNA synthetase. Biochimie (Special Issue “Mitochondria: an organelle for life”) 100, 18-26.

34. Huot, J.L.*, Enkler, L.*, Megel, C., Karim, L. Laporte, D., Becker, H.D.#, Duchêne, A.-M., Sissler, M. #, Maréchal-Drouard, L. # (2014) Idiosyncrasies in decoding mitochondrial genomes. Biochimie (Special Issue “Mitochondria: an organelle for life”) 100, 95-106.

* should be regarded as co-first authors
# should be regarded as co-corresponding authors

35. Maréchal-Drouard, L. #, Sissler, M. #, Tarassov, I. # (2014). Mitochondria: An organelle for life. Biochimie, Special issue. 100, 1-2

# should be regarded as co-corresponding authors

36. Simon, M., Richard, E.M., Wang, X., Shahzad, M., Huang, V.H., Qaiser, T.A., Potluri, P., Mahl, S.E., Davila, A., Nazli, S., Hancock, S., Yu, M., Gargus, J., Chang, R., Al-sheqaih, N., Newman, W.G., Abdenur, J., Starr, A., Hegde, R., Dorn, T., Busch, A., Park, E., Wu, J., Schwenzer, H., Flierl, A., Florentz, C., Sissler, M., Khan, S.N., Li, R., Guan, M.-X., Friedman, T.B., Wu, D.K., Procaccio, V., Riazuddin, S., Wallace, D.C., Ahmed, Z.M., Huang, T., Riazuddin, S. (2015) Mutations of human NARS2, encoding the mitochondrial asparaginyl-tRNA synthetase, cause nonsyndromic deafness and Leigh Syndrome. Plos Genetics. 11(3):e1005097.

37. Sauter, C., Lorber, B., Gaudry, A., Karim, L., Schwenzer, H., Wien, F., Roblin, P., Florentz, C., Sissler, M. (2015) Neurodegenerative disease-associated mutants of a human mitochondrial aminoacyl-tRNA synthetase present individual molecular signatures. Scientific Reports, 5:17332. doi: 10.1038/srep17332.

38. Sissler, M. (2016). What is so special about neuronal translation? (Comment on DOI 10.1002/bies.201600052). BioEssays, 38, 816.

39. Carapito C, Kuhn L, Karim L, Rompais M, Rabilloud T, Schwenzer H, Sissler M (2017) Two proteomic methodologies for defining N-termini of mature human mitochondrial aminoacyl-tRNA synthetases. Methods,113, 111-119. doi: 10.1016/j.ymeth.2016.10.012

40. Moulinier L, Ripp R, Castillo G, Poch O, Sissler M (2017) MiSynPat: an integrated knowledge base linking clinical, genetic, and structural data for disease-causing mutations in human mitochondrial aminoacyl-tRNA synthetases. Human mutation, doi: 10.1002/humu.23277

41. Sissler M, González-Serrano L.E., Westhof E (2017) Recent advances in mitochondrial aminoacyl-tRNA Synthetases and disease. Trends in Molecular Medicine, 23, 693-708.

42. González-Serrano L.E., Karim L., Pierre F, Schwenzer H., Rötig A., Munnich A., Sissler M. (2018) Three human aminoacyl-tRNA synthetases have distinct sub-mitochondrial localizations that are unaffected by disease-associated mutations. J. Biol. Chem. DOI: 10.1074/jbc.RA118.003400. 293, 13604-13615.

43. Hosseini M., Roy P, Sissler M, Zirbel C, Westhof E, Leontis N (2018) How to fold and protect mitochondrial ribosomal RNA with fewer guanines. Nucleic Acids Res. 46, 10946-10968. doi: 10.1093/nar/gky762.

46. Roux C.J., Barcia G., Schiff M., Sissler M., Levy R., Dangouloff-Ros V., Desguerre I., Edvardson S., Elpeleg O., Rötig A., Munnich A., Boddaert N. (2020) Puzzling diversity of brain MRI patterns in mitochondrial aminoacyl-tRNA synthetase mutations. Submitted

45. Soufari H., Waltz F., Parrot C., Durrieu S., Bochler A., Kuhn L., Sissler M., Hashem Y. (2020) Structure of the full kinetoplastids mitoribosome and insight on its large subunit maturation. Submitted (preprint available at https://www.biorxiv.org/content/10.1101/2020.05.02.073890v2.full).

44. González-Serrano L.E., Chihade J.W., Sissler M. (2019) When a common biological role does not imply common disease outcomes: disparate pathology linked to human mitochondrial aminoacyl-tRNA synthetases. J. Biol. Chem. doi: 10.1074/jbc.REV118.002953. 294, 5309-5320.

PhD thesis direction

  • Ligia Elena González-Serrano (September 21st, 2018):

“Caractérisation de l’ArgRS mitochondrial humaine et contribution à la compréhension des pathologies liées aux mutations des aminoacyl-ARNt synthétases mitochondriales”

Thèse de l’Université de Strasbourg

Direction: Marie Sissler

  • Tina Muller-Jühling (December 14th, 2016):

“ARNt « manchots »: structure, fonctionnalité, évolution”

Thèse des Universités de Strasbourg et de Leipzig

Direction: Catherine Florentz and Mario Mörl

Supervision: Marie Sissler and Claude Sauter

  • Loukmane Karim (October 4th, 2016):

“Organisation sous-mitochondriale de l’aspartyl-ARNt synthétase humaine et implication dans le syndrome LBSL”

Thèse de l’Université de Strasbourg

Direction: Marie Sissler

  • Hagen Schwenzer (October 21st, 2013):

“Aminoacyl-ARNt synthetases mitochondriales humaines: aspects fondamentaux et contribution à la compréhension de pathologies reliées”

Thèse de l’Université de Strasbourg

Direction: Marie Sissler and Catherine Florentz

  • Marie Messmer (November 19th, 2008):

“Originalités structurales et fonctionnelles du système d’aspartylation mitochondrial humain”

Thèse de l’Université Louis Pasteur

Direction: Catherine Florentz

Supervision: Marie Sissler

  • Aurélie Fender (November 18th, 2005):

“Etude comparative de couples ARNt/aminoacyl-ARNt synthétases chez la levure et la mitochondrie humaine”

Thèse de l’Université Louis Pasteur

Direction: Catherine Florentz

Supervision: Marie Sissler

  • Marie Sissler (11 février 1998):

“Contribution à la compréhension de la spécificité d’aminoacylation de l’ARNtArg de levure.”

Thèse de l’Université Louis Pasteur

Direction: Catherine Florentz