Background

Vordiplom in Biology (equivalent to BSc, 1988), Diplom in Microbiology, Genetics, Biochemistry & Immunology (equivalent to MSc, 1992), joint programme offered by Leibniz University, Medical School & Veterinarian School, Hannover, Germany; PhD in Genetics and Molecular Biology (1996), Leibniz University, Hannover, Germany; Postdoc & Adjunct Scientist (1996 - 2005), National Institutes of Health, Bethesda, USA; Senior Lecturer (since 2005), Massey University

Teaching

122.101/221 - Biochemistry of Cells/Foods 122.233 - Metabolic Biochemistry (paper coordinator)
162.101 - Cell Biology
203.203 - Human Genetics
203.341 - Genetics and Evolution
122.704 - Molecular Cell Biology (paper coordinator)
203.761 - Molecular Evolution (paper coordinator)

Research Interests

• Signal transduction mechanisms, stress response, and translational control
• Using Saccharomyces as model organism for health related questions
• Saccharomyces in Biotechnological applications
• Organisms: Saccharomyces cerevisiae, Neurospora crassa, Escherichia coli, cell culture, etc
• Techniques applied: Molecular Biology, Molecular Genetics, Genetics, Cell Biology, Biochemistry (protein purification,
protein-protein/nucleic acid interactions, ribosomes, enzyme assays)

More information is available about my research and postgraduate
student opportunities on my lab website, http://sattlegger-lab.webs.com

Selected Publications

Evidence that eukaryotic translation elongation factor 1A (eEF1A) binds the Gcn2 C-terminus and inhibits Gcn2 activation. * (2011) Visweswaraiah J, Lageix S, Castilho BA, Izotova L, Kinzy TG, Hinnebusch AG, and Sattlegger E. J. Biol. Chem. 286(42):36568-36579.  * selected as 'Paper of the Week', in the week of 21 October 2011, (selected by JBC's Associate Editors and Editorial Board Members as representing the top 1% of papers reviewed in terms of significance and overall importance).see http://www.jbc.org/potw and http://www.jbc.org/content/286/42/e99968.short

Gcn1 and actin binding to Yih1: Implications for activation of the eIF2 kinase Gcn2.  (2011)  Sattlegger* E (*correponding author), Barbosa JARG, Moraes MCS, Martins RM, Hinnebusch AG, Castilho BA. J. Biol. Chem. 286(12):10341-55

Generating highly concentrated yeast whole cell extract using low-cost equipment. (2011) Visweswaraiah J, Dautel M, & Sattlegger E. Nature Protocol Exchange. doi:10.1038/protex.2011.212

Saccharomyces cerevisiae Rbg1 protein and its binding partner Gir2 interact on Polyribosomes with Gcn1.  (2009) Wout PK, Sattlegger E, Sullivan SM, Maddock JR.  Eukaryot Cell. 8(7):1061-71.

Yeast Studies Reveal New Roles for an Ancient Skeleton.  (2009)
Munn A & Sattlegger E.  Australian Biochemist.  40(8):8,9-13. review 
Sattlegger moved to New Zealand, applied for funding, and established own research group, therefore leading to a 'publication gap'.

 Interplay between GCN2 and GCN4 expression, translation elongation factor 1 mutations and translational fidelity in yeast.  (2005) Magazinnik T, Anand M, Sattlegger E, Hinnebusch AG, Kinzy TG.  Nucleic Acids Res. 33(14):4584-92.

IMPACT, a protein preferentially expressed in the mouse brain, binds GCN1 and inhibits GCN2 activation.  (2005) Pereira CM, Sattlegger E, Jiang HY, Longo BM, Jaqueta CB, Hinnebusch AG, Wek RC, Mello LE, Castilho BA.  J Biol Chem. 280(31):28316-23.

Polyribosome binding by GCN1 is required for full activation of eukaryotic translation initiation factor 2alpha kinase GCN2 during amino acid starvation.* Sattlegger E, Hinnebusch AG.  J Biol Chem. 280(16):16514-21.   * listed in Faculty of 1000 Biology, see http://f1000.com/signin?target=1024423 

YIH1 is an actin-binding protein that inhibits protein kinase GCN2 and impairs general amino acid control when overexpressed.  (2004) Sattlegger E, Swanson MJ, Ashcraft EA, Jennings JL, Fekete RA, Link AJ, Hinnebusch AG.  J Biol Chem. 279(29):29952-62.

Biophysical characterization of Gir2, a highly acidic protein of Saccharomyces cerevisiae with anomalous electrophoretic behavior.  (2004) Alves VS, Pimenta DC, Sattlegger E, Castilho BA.  Biochem Biophys Res Commun. 314(1):229-34.

Separate domains in GCN1 for binding protein kinase GCN2 and ribosomes are required for GCN2 activation in amino acid-starved cells.  (2000) Sattlegger E, Hinnebusch AG.  EMBO J. 19(23):6622-33.

The WD protein Cpc2p is required for repression of Gcn4 protein activity in yeast in the absence of amino-acid starvation.  (1999) Hoffmann B, Mösch HU, Sattlegger E, Barthelmess IB, Hinnebusch A, Braus GH.  Mol Microbiol. 31(3):807-22.

cpc-3, the Neurospora crassa homologue of yeast GCN2, encodes a polypeptide with juxtaposed eIF2alpha kinase and histidyl-tRNA synthetase-related domains required for general amino acid control.  (1998) Sattlegger E, Hinnebusch AG, Barthelmess IB.  J Biol Chem. 273(32):20404-16.

The cpc-2 gene of Neurospora crassa encodes a protein entirely composed of WD-repeat segments that is involved in general amino acid control and female fertility.  (1995) Müller F, Krüger D, Sattlegger E, Hoffmann B, Ballario P, Kanaan M, Barthelmess IB.  Mol Gen Genet. 248(2):162-73.