GEORG JANDER - Boyce Thompson Institute

CURRICULUM VITAE
GEORG JANDER
GEORG JANDER
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Title: Assistant Scientist
Address: Boyce Thompson Institute for Plant Research
Tower Road, Ithaca, NY 14853
Phone: 607-254-1365
Fax: 607-254-2958
Email: gj32@cornell.edu
Education and Professional Experience:
2002-present Assistant Scientist, Boyce Thompson Institute
1998-2002 Scientist, Cereon Genomics, Cambridge, MA
1996-1998 Postdoctoral Fellow, Massachusetts General Hospital
(Advisor: Fred Ausubel)
1988-1995 Ph.D., Harvard Medical School, Microbiology
(Advisor: Jon Beckwith)
1983-1987 B. S., Washington University, St. Louis, MO
Honors and Professional Recognition:
1996-1997 NIH Postdoctoral Fellowship
1994 Office of Naval Research Fellowship, Microbial Diversity Class,
Marine Biological Laboratories, Woods Hole
1988-1990 National Science Foundation Graduate Fellowship
1983-1987 National Merit Scholar
1983-1987 Woodward Scholarship for Engineering
Professional Affiliations:
Entomological Society of America
American Society for Plant Biology
American Association for the Advancement of Science
Institutional and Academic Service:
Current and Recent Boyce Thompson Institute/Cornell Committees
Member, BTI Distinguished Lecture Committee
Chair, BTI Plant Growth Facilities Committee
Member, BTI Faculty Search Committee
Other
Reviewer for: Genetics, Plant Physiology, Plant Journal, Proceedings of the National Academy of
Sciences, Nucleic Acids Research, Genome Research, New Phytologist, National Science Foundation,
USDA-ARS, Israeli Science Foundation
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GEORG JANDER
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Publications:
Braun V., B. Neuss, Y. Ruan, E. Schiebel, H. Schoeffler, and G. Jander. 1987. Identification of the Serratia
marcescens hemolysin determinant by cloning into Escherichia coli. J. Bacteriology 169:2113-2120.
DiRita V. J., C. Parsot, G. Jander, and J. J. Mekalanos. 1991. Regulatory cascade controls virulence in Vibrio
cholerae. Proc. Natl. Acad. Sci. USA 88:5403-5407.
Boyd D., B. Traxler, G. Jander, W. Prinz, and J. Beckwith. 1993. Gene fusion approaches to membrane protein
topology. Society of General Physiologists Series 48:22-37.
Bardwell J. C. A., J. O. Lee, G. Jander, N. L. Martin, D. Belin, and J. Beckwith. 1993. Pathways of disulfide
bond formation of proteins in vivo. In: Molecular Biology of Phosphate in Microorganisms, A. M. Torriani,
S. Silver, and E. Yagil, eds.
Jander, G., N. L. Martin, and J. Beckwith. 1994. Two cysteines in each periplasmic domain of the membrane
protein DsbB are required for its function in protein disulfide bond formation. EMBO J. 13:5121-5127.
Guilhot, C., G. Jander, N. L. Martin, and J. Beckwith. 1995. Evidence that the pathway of disulfide bond
formation in Escherichia coli involves interactions between cysteines of DsbA and DsbB. Proc. Natl. Acad.
Sci. USA 92:9895-9899.
Jander, G., J. E. Cronin, and J. Beckwith. 1996. Biotinylation in vivo as a sensitive indicator of protein secretion
and membrane protein insertion. J. Bacteriology 178:3049-3058.
Jander, G., L. G. Rahme, and F. M. Ausubel. 2000. Positive correlation between virulence of Pseudomonas
aeruginosa mutants in mice and insects. J. Bacteriology 182:3843-3845.
Jander, G., J. Cui, B. Nhan, N. Pierce, and F. M. Ausubel. 2001. The TASTY locus on chromosome 1 of
Arabidopsis thaliana affects feeding of the insect herbivore Trichoplusia ni. Plant Physiol. 126:890-898.
Jander, G., S. R. Norris, S. D. Rounsley, D. F. Bush, I. M. Levin, and R. L. Last. 2002. Arabidopsis map-based
cloning in the post-genome era. Plant Physiol. 129:440-450.
Cui, J., G. Jander, L. R. Racki, P. D., Kim, F. M. Ausubel, and N. Pierce. 2002. Signals involved in Arabidopsis
resistance to Trichoplusia ni caterpillars induced by virulent and avirulent strains of the phytopathogen
Pseudomonas syringae. Plant Physiol. 129:551-564.
Jander, G., S. Baerson, J. A. Hudak, K. A. Gonzalez, K. J. Gruys, and R. L. Last. 2003. Ethylmethanesulfonate
saturation mutagenesis in Arabidopsis to determine frequency of herbicide resistance. Plant Physiol.
131:139-146.
Jander, G., S. R. Norris, V. Joshi, M. Fraga, A. Rugg, S. Yu, L. Li, and R. L. Last. 2004. Application of a highthroughput
HPLC-MS/MS assay to Arabidopsis mutant screening; evidence that threonine aldolase plays a
role in seed nutritional quality. Plant J. 39:465-475.
Kim, J.-H., T. P. Durrett, R. L. Last, and G. Jander. 2004. Characterization of the Arabidopsis TU8
glucosinolate mutation, an allele of TERMINAL FLOWER2. Plant Mol. Biol. 54:671-682.
Jander, G. 2004. Gene identification and cloning by molecular marker mapping. In: Arabidopsis Protocols, 2 nd
edition, J. Sanchez-Serrano, ed. Humana Press, Totowa, NJ, in press.
Bush, J., G. Jander, and F. M. Ausubel. 2004. Prevention and control of pests and diseases in Arabidopsis. In:
Arabidopsis Protocols, 2 nd edition, J. Sanchez-Serrano, ed. Humana Press, Totowa, NJ, in press.
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GEORG JANDER
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Patents/Patent Applications:
G. Jander, US Patent 6,594,977, “Seed Collector”, issued 7/22/2003.
Research Interests:
Arabidopsis-aphid Interactions
The interactions between plants and insect herbivores
constitute a fascinating, co-evolved natural system. Plants
produce a wide variety of toxins, repellents, and physical
barriers to keep from being eaten. Insects, on the other hand,
manage to circumvent these barriers, develop resistance, and
sometimes even co-opt plant defensive compounds as an
attractive signal. Although specific insect attractants and
repellents have been identified in many plant species,
relatively little is known about the genetic regulation of their
production.
Arabidopsis thaliana (Arabidopsis) is an excellent model
plant for studying the genetic basis of insect defense. The small size, rapid generation time, and selfpollinating
nature of this plant permit the mutant screens and genetic mapping that we are undertaking.
Map-based cloning of interesting genes is facilitated by the small genome size of Arabidopsis and the
extensive DNA sequence and genetic linkage data that are available. In addition, there are publicly
available collections of hundreds of mutants and ecotypes (natural isolates) from around the world.
As an insect model, we are using Myzus persicae (peach-potato aphid), which feeds on Arabidopsis
and hundreds of other species from more than 40 plant families. M. persicae is also the world's number
one transmitter of viruses to crop plants. Because of its agricultural importance, world-wide distribution,
rapid growth, and ease of lab culture, M. persicae is a common research subject and probably the most
extensively studied aphid. Aphids are a particularly attractive research model because of their
parthenogenetic life cycle, which allows replication of experiments with genetically identical insects.
Arabidopsis Mutants with Altered Glucosinolate Biosynthesis
Research on the insect defenses of Arabidopsis and other The glucosinolate-myrosinase defense system of crucifers
Brassicaceae has focused primarily on the
glucosinolate/myrosinase system. This is a resident binary system
in which glucosinolates and the enzyme myrosinase are stored in
R is derived from
amino acids, with
modifications
Glucosinolates
S Glucose
R
-
NOSO 3
Myrosinase
separate compartments of the plant cells. When the plants are
Herbivory
damaged, the enzyme myrosinase cleaves the glucosinolates,
causing the release of thiocyanates and other volatiles that are
distasteful to many generalist herbivores such as Trichoplusia ni
Glucosinolates
SH
R
-
NOSO 3
Myrosinase
Glucose
(cabbage looper). On the other hand, crucifer-feeding specialists
such as Plutella xylostella (diamondback moth) are often attracted
by glucosinolates and their degradation products.
R-N=C=S
Isothiocyanate
R-S-C R-S-C N N
Thiocyanate
R-C N
Nitrile
S
N
Epithionitrile
Some crucifer-feeding specialists, for instance Brevicoryne brassicae (cabbage aphid), are not only
resistant to glucosinolates, but have co-opted this plant defense system to make themselves more resistant
to predators. M. persicae avoids degradation of glucosinolates when feeding on crucifers, and they appear
essentially unchanged in the aphid honeydew.
The side chains of Arabidopsis glucosinolates are derived from methionine, tryptophan, or
phenylalanine, with additional modifications occurring after the addition of the amino acid. Over 100
different glucosinolates are known from the Brassicaceae and more than 30 are found in Arabidopsis. It is
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GEORG JANDER
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assumed that the plants make such a variety of glucosinolates because they play different roles in defense
against herbivores and perhaps also fungi and bacteria. However, due to the binary nature of the
glucosinolate/myrosinase system and the volatile breakdown products, it has not been possible to
adequately test the effects of individual glucosinolates in an in vitro feeding assay.
One way to test the effects of individual glucosinolate varieties on insect herbivory is to make
mutants affecting only one or a small class of glucosinolates. Such mutant lines could then be compared
to isogenic wild type lines in insect feeding experiments. We used a high-throughput HPLC assay to
screen 5000 Arabidopsis EMS mutant lines for alterations in glucosinolate levels. This screen identified a
total of thirty mutants with either qualitative or quantitative differences in glucosinolates content. We are
continuing to characterize these mutants and will use them in further experiments to study the effects of
individual glucosinolates on insect feeding behavior.
Arabidopsis Mutants with Altered Amino Acid Biosynthesis
A population of 10,000 EMS-mutagenized Arabidopsis
lines was screened by HPLC/MS for altered levels of free
43 mutants with increased Asp-derived amino acids
amino acids in seeds. Among these, 43 lines had heritable
90
increases (2 to 80-fold) of one or more of aspartate-derived
80
amino acids threonine, methionine, lysine, and isoleucine.
70
60
We are using map-based cloning to identify the mutations
50
that are responsible for these amino acid phenotypes.
40
30
One mutant that is being investigated has a defect in
20
threonine aldolase, which converts threonine to glycine and
10
0
acetaldehyde. A block in this enzymatic step causes a 20-fold
Ile Lys Met Thr
increase in seed threonine content. Similar mutations in
Affected amino acid
threonine aldolase of crops plants could be used to increase their seed threonine content and nutritional
value.
Development of a Glass Slide Microarray for Arabidopsis Genotyping
To map mutations in F2 populations and to create genetic maps of recombinant inbred (RI) line
populations, the genotype of individual plants has to be determined using several hundred genetic
markers. Array-based genotyping allows simultaneous assessment of many molecular markers, ultimately
suggesting this approach as the fastest and most cost-effective genotyping method. Studies in yeast have
demonstrated the feasibility of array-based genotyping employing single nucleotide polymorphisms
(SNPs). As the larger genome size of Arabidopsis complicates SNP-based genotyping, a spotted
oligonucleotide genotyping array based on insertion/deletion differences between the Columbia (Col-0)
and Landsberg erecta (Ler) Arabidopsis accessions is being developed. Most of the expected 500 marker
elements of this array will come from the Monsanto Arabidopsis Polymorphism Collection. The utility of
the array will be demonstrated by creating genetic maps of at least four sets of recombinant inbred lines
and by mapping mutations in two F2 populations. The identity of the informative oligonucleotides and
marker data for recombinant inbred lines will be placed in a public database.
This project is funded by grant #0313473 from the National Science Foundation to Georg Jander
(Boyce Thompson Institute for Plant Research), Duccio Cavalieri (Bauer Center for Genome Research),
and Christine Queitsch (Bauer Center for Genome Research).
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4
Fold increase over wild type
(Average of 4 or 8 measurements)