Selected publications
* denotes corresponding author
Experimentally
based structural model of Yih1 provides insight into its function in
controlling the key translational regulator Gcn2. Elena Harjes,
Geoffrey B Jameson, Yi‐Hsuan Tu, Natalie Burr, Trevor
S Loo, Alexander K Goroncy, Patrick JB Edwards, Stefan Harjes, Ben Munro,
Christoph Göbl, Evelyn Sattlegger, Gillian E Norris. FEBS
letters, in press
Domain II of the translation elongation factor eEF1A is required for Gcn2 kinase inhibition. (2020) Ramesh R & Sattlegger E. FEBS Lett. 2020 594:2266-81. Online ahead of print. Publication highlighted on the Journal?s website and promoted by the Journal through twitter.
Damaging
de novo missense variants in EEF1A2 lead to a developmental and degenerative epileptic-dyskinetic
encephalopathy. (2020) Carvill GL, Padilla-Lopez S, Helbig KL,
Myers C, Guida BS, Sebe J, Huether R, Kruer TN, Oktay SU, Ramsey K, Narayanan
V, Feyma T, Tang S, Stickney H, Bandiwad AA, Sisneros JA, Rohena LO,
Hollingsworth G, Jones C, Gill D, Depienne C, Nava C, Lin AE, Jansen FE, Vissers
L, Willemsen MH, Kleefstra T, Sadleir LG, Sattlegger E, Sheffer I,
Raible D, Mefford H,* Kruer MC* Human Mutation 41:1263-1279. Editor's Choice paper, considered
particularly noteworthy by journal?s editorial board, will be available, at
https://onlinelibrary.wiley.com/doi/toc/10.1002/(ISSN)1098-1004.HUMU-Editors-Choice
Yeast as a model to
understand actin-mediated cellular functions in mammals - illustrated with four
actin cytoskeleton proteins. (2020) Akram Z, Ahmed I, Mack H, Kaur R, Silva R, Castilho B,
Friant S, Sattlegger E, Munn A. invited review, Cells 9(3):672
Persistent contamination of Salmonella, Campylobacter, Escherichia
coli, and Staphylococcus aureus at
a broiler farm in New Zealand. (2020) Castaneda-Gulla K,
Sattlegger E, Mutukumira AN. Can J Microbiol. 2020 66(3):171-185. Selected as 'Editors'
Choice' paper. This initiative of Canadian Science
Publishing and the Journal is a means of highlighting articles
of particularly high caliber and topical
importance. https://www.nrcresearchpress.com/journal/cjm
Imprinted and ancient
Gene: a potential mediator of cancer cell survival during tryptophan
deprivation. (2018) Tomek P, Gore SK, Potts CL, Print CG, BLack MA, Hallemayr
A, Killan M, Sattlegger E, Ching LM. Cell Communication and
Signalling.16(1):88 https://rdcu.be/bbTL2
A Rapid Extraction Method for
mammalian cell cultures, suitable for quantitative immunoblotting analysis of
proteins, including phosphorylated GCN2 and eIF2alpha. (2017)
Silva RC, Castilho BA, Sattlegger E*. MethodsX. 5:75-82 https://doi.org/10.1016/j.mex.2017.10.008
Cost-effective and rapid lysis of Saccharomyces cerevisiae
cells for quantitative western blot analysis of proteins, including
phosphorylated eIF2alpha. (2017) Lee SJ, Ramesh R, de Boor V, Gebler JM,
Silva RC, Sattlegger E*. Yeast. 34(9):371-382
Recognition of a structural
domain (RWDBD) in Gcn1 proteins that interacts with the RWD domain containing
proteins. (2017) Rakesh R, Krishnan R, Sattlegger E*,
Srinivasan N*. Biology Direct 2017 12:12, DOI:10.1186/s13062-017-0184-3
Perturbations in actin
dynamics reconfigure protein complexes that modulate GCN2 activity and promote
an eIF2 response. (2016) Silva RC, Sattlegger E, Castilho BA. J. Cell Sci. 29(4):4521-4533 selected
for inclusion in the 'In This Issue' section of JCS, http://jcs.biologists.org/content/129/24/e2404, demonstrating international
recognition of our research finding. featured in Journal issue http://jcs.biologists.org/content/129/24/e2404
Re-using
plastic cassettes for vertical gel electrophoresis. (2016) Ramesh R, Gebler JM, de Boor V,
Sattlegger E.* Nature Protocol Exchange. doi: 10.1038/protex.2016.041
The Gcn2 Regulator Yih1 Interacts with the Cyclin Dependent Kinase
Cdc28 and Promotes Cell Cycle Progression through G2/M in Budding Yeast. (2015) Silva RC, Dautel M, Di Genova BM, Amberg DC,
Castilho BA,* Sattlegger E*. PLoS One. 10(7):e0131070.
Gcn1 contacts the small ribosomal protein Rps10, which is
required for full activation of the protein kinase Gcn2. (2015)
Lee SJ, Swanson MJ, and SattleggerE, Biochem J. 466:547-59
Yeast
studies reveal moonlighting functions of the ancient actin cytoskeleton. (2014) Sattlegger
E, Chernova TA, Gogoi NM, Pillai IV, Chernoff YO, and Munn* AL. peer-reviewed
review. IUBMB Life 66:538-45
Keeping the eIF2 alpha kinase Gcn2 in check. (2014) Castilho BA, Shanmugam R, Silva RC, Ramesh R,
Himme BM, Sattlegger* E. invited peer-reviewed review. BBA Molecular Cell
Research. 1843:1948-68. doi:10.1016/j.bbamcr.2014.04.006
Free access until 7/8/2014: http://authors.elsevier.com/a/1PD9Nc5IDEGrS
Evolutionarily conserved IMPACT impairs various
stress responses that require GCN1 for activating the eIF2 kinase GCN2. (2014) Cambiaghi TD, Pereira CM, Shanmugam R,
Bolech M, Wek RC, Sattlegger E, Castilho* BA. Biochem. Biophys. Res. Commun.
443:592-7
Semi-quantitative Colony Immunoassay for determining and optimizing
protein expression inSaccharomyces
cerevisiae and Escherichia coli. (2014) Cridge AG, Visweswaraiah J, Ramesh
R, Sattlegger* E. Anal. Biochem. 447:82-9
Transcriptional defect of an inherited NKX2-5
haplotype comprising a SNP, a nonsynonymous and a synonymous mutation,
associated with human congenital heart disease. (2013)
Reamon-Buettner SM, Sattlegger E, Ciribilli Y, Inga
A, Wessel A, and Borlak* J. PLoS ONE 8(12) e83295. DOI:
10.1371/journal.pone.0083295
Simultaneous
semi-dry electrophoretic transfer of a wide range of differently sized proteins
for immunoblotting. (2013)
Wiedemann M, Lee SJ, Silva RC, Visweswaraiah J, Soppert J, & Sattlegger* E.
Nature Protocol Exchange. doi: 10.1038/protex.2013.095
Overexpression of Eukaryotic
Translation Elongation Factor 3 (eEF3) impairs Gcn2 activation. (2012) Visweswaraiah J, Lee SJ, Hinnebusch AG, and
Sattlegger* E. J. Biol. Chem. 287: 37757-37768.
doi:10.1074/jbc.M112.368266
Evidence
that Yih1 resides in a complex with ribosomes. (2012) Waller T, Lee SJ, and Sattlegger E. The FEBS J.
279(10):1761-76
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 (at that time) 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.
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