Alexandra Lusser Ph.D., Assoc. Prof.

EMail: alexandra.lusser@i-med.ac.at
Tel.: +43/(0)512/9003-70210
Fax: +43/(0)512-9003-73100

Research group

Chromatin and Epigenetics Laboratory

Alexandra Lusser

Short curriculum

1998 Ph.D. thesis on enzymes involved in chromatin modification; Department of Microbiology, Medical School, University of Innsbruck
1998 Höchst Preis (Scientific Award)
2001-2004 Award of the APART (AUSTRIAN PROGRAMME FOR ADVANCED RESEARCH AND TECHNOLOGY) fellowship of the Austrian Academy of Sciences. Division of Biology, Section of Molecular Biology, University of California, San Diego.
2004 Assistant Professor, Department of Molecular Biology, Innsbruck Medical University.
2005-2011 START-grant from the bm:wk.
April 2008 Habilitation (Venia docendi) for Molecular Biology.
2008- Associate Professor, Department of Molecular Biology, Innsbruck Medical University.

Research interests

The way in which eukaryotic DNA is organized in chromatin has profound effects on all processes that direct DNA metabolism (such as transcription, replication, repair and recombination). We are interested to learn how the establishment and maintenance of eukaryotic chromatin affects those processes. We are approaching this question by studying the molecular mechanism and biological context of the chromatin assembly process.

Chromatin assembly is a fundamentally important process that is tightly linked to DNA replication and enables the cell to faithfully duplicate the chromosomes. In addition, chromatin assembly occurs independently of replication to turn-over histones, for instance during transcription or DNA damage repair. We have recently identified Drosophila CHD1 as an ATP-dependent chromatin assembly factor that belongs to the SNF2 superfamily of ATPases. Many members of this large group of molecular motor proteins are involved in the modification of chromatin structure. Only members of two SNF2-subfamilies, namely CHD1, and the previously identified ISWI are known to catalyze the ATP-dependent assembly of chromatin. ISWI and its human homolog hSNFH function as part of the Drosophila ACF and CHRAC chromatin assembly complexes and the human RSF complex, whereas Drosophila CHD1 appears to predominantly operate as a monomer. CHD1 and ACF enzymes catalyze the ATP-dependent assembly of periodic arrays of nucleosomes. Interestingly, these enzymes generate different types of chromatin in terms of internucleosomal spacing distance and linker histone H1 content.

We are particularly interested in the biological functions of CHD1, which has been implicated in the regulation of transcriptional elongation and termination processes. To study the implications of chromatin assembly in processes of DNA metabolism , we use a biochemical approach employing in vitro chromatin reconstitution and transcription systems. In addition, chromatin assembly defects are investigated in tissue culture as well as in mutant Drosophila lines.

Teaching

From the online catalog of the Innsbruck Medical University (in German): Current lectures

From the online catalog of the University of Innsbruck (in German): Current lectures

Publications

  1. Sebald, J., Morettini, S., Podhraski, V., Lass-Flörl, C., Lusser, A. (2012) CHD1 contributes to intestinal resistance against infection by P. aeruginosa in Drosophila melanogaster. PLoS ONE, 7(8): e43144.

  2. Fischnaller, S., Dowell, F., Lusser, A., Schlick-Steiner, B., Steiner, F.M. (2012) Non-destructive species identification of Drosophila obscura and D. subobscura (Diptera) using near-infrared spectroscopy. Fly (Austin) 6(4): 1-6

  3. Piatti, P.; Zeilner, A.; Lusser, A. (2011) ATP-Dependent Chromatin Remodeling Factors and Their Roles in Affecting Nucleosome Fiber Composition. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. 12(10); 6544-6565.

  4. Morettini, S., Tribus, M., Zeilner, A., Campo-Fernandez, B., Sebald, J., Scheran, G., Wörle, H., Podhraski, V., Fyodorov, D., Lusser, A. (2011). The chromodomains of CHD1 are critical for enzymatic activity but less important for chromatin localization. Nucl. Acids Res. 39(8); 3103-3115.

  5. Podhraski V, Campo-Fernandez B, Woerle H, Piatti P, Niederegger H, et al. (2010) CenH3/CID Incorporation Is Not Dependent on the Chromatin Assembly Factor CHD1 in Drosophila. PLoS ONE 5(4): pp. e10120. doi:10.1371/journal.pone.0010120

  6. Morettini, S., Podhraski, V., Lusser, A. (2008). ATP-dependent chromatin remodeling enzymes and their various roles in cell cycle control. Front Biosci. 13, 5522-32.

  7. Konev, A.Y, Tribus, M., Podhraski, V., Park, S.Y., Lim, C.Y., Emelyanov, A.V., Vershilova, E., Pirrotta, V., Kadonaga, J.T., Lusser, A., Fyodorov, D.V. (2007). The CHD1 motor protein is required for deposition of histone H3.3 into chromatin in vivo. Science 317, 1087-1090.

  8. Lusser, A., Urwin, D.L., Kadonaga, J.T. (2005). Distinct Activities of CHD1 and ACF in ATP-dependent chromatin assembly. Nat. Struct. Mol. Biol. 12, 160-166.

  9. Lusser, A., Kadonaga, J.T. (2004). Strategies for the reconstitution of chromatin. Nat. Methods 1, 19-26.

  10. Alexiadis, V., Lusser, A., Kadonaga, J.T.(2004). A conserved N-terminal motif in Rad54 is important for chromatin remodeling and homologous strand pairing. J. Biol. Chem. 279, 27824-27829.

  11. Lusser, A., and Kadonaga, J.T. (2003). Chromatin remodeling by ATP-dependent molecular machines. BioEssays 25, 1192-1200.

  12. Pipal, A., Goralik-Schramel, M., Lusser, A., Lanzanova, C., Sarg, B., Loidl, A., Lindner, H., Rossi, V. & Loidl, P. (2003). Regulation and Processing of Maize Histone Deacetylase HDA1 by Limited Proteolysis. Plant Cell 15, 1904-1917.

  13. Lusser, A. (2002). Acetylated, methylated, remodeled: chromatin states for gene regulation.Curr. Opin. Plant Biol. 5, 437-443.

  14. Rossi, V., Locatelli, S., Lanzanova, C., Boniotti, B., Varotto, S., Pipal, A., Goralik-Schramel, M., Lusser, A., Glatz, C., Gutierrez, C. and Motto, M. (2003). A maize histone deacetylase and retinoblastoma-related protein physically interact and cooperate in repressing gene transcription. Plant. Mol. Biol. 51, 401-413.

  15. Brandtner, E.M., Lechner, T., Loidl, P. and Lusser, A. (2002). Molecular identification of PpHDAC1, the first histone deacetylase from the slime mold physarum polycephalum. Cell Biol. Int. 26, 783-789.

  16. Dangl, M., Brosch, G., Haas, H., Loidl, P. and Lusser, A. (2001) Comparative analysis of HD2 type histone deacetylases in higher plants.Planta 213, 280-285.

  17. Lusser, A., Kölle, D. and Loidl, P. (2001) Histone acetylation: Lessons from the plant kingdom.Trends in Plant Science 6, 59-65.

  18. Lechner, T., Lusser, A., Pipal, A., Brosch, G., Loidl, A., Goralik-Schramel, M., Sendra, R., Wegener, S., Walton, J. D., and Loidl, P. (2000). RPD3-Type Histone Deacetylase in Maize Embryos. Biochemistry, 39, 1683-1692.

  19. Lusser, A., Eberharter, A., Loidl, A., Goralik-Schramel, M., Horngacher, M., Haas, H. and Loidl, P. (1999). Analysis of the histone acetyltransferase B complex of maize. Nucleic Acids Res. 27, 4427-4435.

  20. Dangl, M., Lusser, A., Brosch, G., Loidl, A., Haas, H. and Loidl, P. (1998) Second Family of Histone Deacetylases. Science 280, 1167.

  21. Kolle, D., Brosch, G., Lechner, T., Lusser, A., and Loidl, P. (1998). Biochemical methods for analysis of histone deacetylases. Methods 15, 323-331.

  22. Lusser, A., Brosch, G., Loidl, A., Haas, H., and Loidl, P. (1997). Identification of maize histone deacetylase HD2 as an acidic nucleolar phosphoprotein. Science 277, 88-91.

  23. Lusser, A., Brosch, G., Lopez-Rodas, G., and Loidl, P. (1997). Histone acetyltransferases during the cell cycle and differentiation of Physarum polycephalum. Eur. J. Cell Biol. 74, 102-110.

  24. Brosch, G., Lusser, A., Goralik-Schramel, M., and Loidl, P. (1996). Purification and characterization of a high molecular weight histone deacetylase complex (HD2) of maize embryos. Biochemistry 35, 15907-15914.

  25. Lechner, T., Lusser, A., Brosch, G., Eberharter, A., Goralik-Schramel, M., and Loidl, P. (1996). A comparative study of histone deacetylases of plant, fungal and vertebrate cells. Biochim. Biophys. Acta 1296, 181-188.

Division of Molecular Biology
(formerly Department of Molecular Biology)
Innsbruck Medical University
Innrain 80-82, A-6020 Innsbruck, Austria
Tel: +43-512-9003-70201, Fax: +43-512-9003-73100
E-Mail: mol-biol@i-med.ac.at

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