Elisabeth Gantt
Emerita and Distinguished University Professor
Member, National Academy of Sciences, U.S.A.
Ph.D., Northwestern University, 1963
Telephone: (301) 405-1649
Fax: (301) 314-9489
E-mail:
egantt@umd.edu
Research Interests: Plant Cell and Molecular Biology, Plant Physiology
Carotenoids play essential roles in protecting organisms against potential
lethal photo-oxidative damage. In photosynthesis they function in harvesting
light for photosynthesis, but also in the dissipation of energy under conditions
of excess light. The biosynthetic pathway of carotenoids in oxygen-evolving
plants is being studied in photosynthetic microalgae as model systems.
Molecular probes for genes encoding several enzymes in the carotenoid biosynthetic
pathway are being used in studying the expression of genes (phytoene synthase,
phytoene desaturase, and lycopene cyclase) during the induction and accumulation
of carotenoid pigments in photosynthetic microalgae that are hyperaccumulators
of carotenoids under environmental stress conditions.
Success of photosynthetic organisms in natural habitats is dependent
upon the organisms' ability to adjust to varying environmental conditions.
The uniqueness of the photosynthetic pigment complexes in red algae is
being studied prompted by our recent finding of chlorophyll- binding proteins
similar to those of green plants. We are studying the structure, function,
regulation, and biosynthesis of the complex using immunological, molecular,
and biochemical approaches.
Recent Publications:
Grabowski, B., S. Tan, F.X. Cunningham, and E. Gantt. 2000. Characterization
of the Porphyridium cruentum Chl a-binding LHC by in vitro reconstitution: LHCaR1
binds 8 Chl a molecules and proportionately more carotenoids than CAB proteins.
Photosyn. Res. 63: 85-96.
Cunningham, F.X., and E. Gantt. 2000. Identification of multi-gene families
encoding isopentenyl diphosphate isomerase in plants by heterologous complementation
in Escherichia coli. Plant and Cell Physiol. 41: 119-123.
Ershov, Y., R.R. Gantt, F.X. Cunningham, and E. Gantt. 2000. Isopentenyl diphosphate
isomerase deficiency in Synechocystis sp. strain PCC6803. FEBS Letters.
473: 337-340.
Cunningham, F.X., T. Lafond, and E. Gantt. 2000. A possible role for LYTB in
the non- mevalonate pathway of isoprenoid biosynthesis. J. Bacteriol.
182: 5841-5848.
Grabowski, B., F.X. Cunningham, Jr., and E. Gantt. 2001. Chlorophyll and carotenoid
binding in a simple red algal LHC crosses phylogenetic lines. Proc. Natl.
Acad. Sci. (USA) 98: 2911-2916.
Cunningham, F.X., Jr. and E. Gantt. 2001. One ring or two? Determination of
ring number in carotenoids by lycopene -cyclase. Proc. Natl. Acad. Sci. (USA)
98: 2908-2910.
Ershov, Y., R. R.
Gantt, F. X. Cunningham,Jr. and E.Gantt. 2002. Isoprenoid biosynthesis
in Synechocystis PCC6803 is stimulated by compounds of the
pentose phosphate cycle but not by pyruvate and
deoxyxylulose-5-phosphate. J. Bact. 184:5045-5051.
Cunningham, F. X., Jr. and E. Gantt. 2002.
Molecular control of floral pigmentation: Carotenoids. pp. 273-293.
In: A. Vainstein (ed.) Breeding for Ornamentals-classical and
Molecular Approaches. Kluwer Academic Publishers, The Netherlands.
Gantt, E., B.
Grabowski, and F. X. Cunningham, Jr. 2003. Antenna systems of red
algae: phycobilisomes with photosystem II and chlorophyll complexes
with photosystem I. pp. 307-322. In: B. R. Green and W.W. Parson
(eds.) Light -Harvesting Antennas in Photosynthesis. Kluwer
Academic Publishers, The Netherlands.
Poliquin, K.
Ershov, Y., F. X. Cunningham, Jr., T. Woreta, R.R. Gantt and E.
Gantt. 2004. Inactivation of sll1556 in Synechocystis PCC 6803
impairs isoprenoid biosynthesis from pentose phosphate cycle
substrates in vitro. J. Bact. 186: 4685-4693.
Cunningham, F. X.
and E. Gantt. 2005 A study in scarlet: enzymes of ketocarotenoid
biosynthesis in the flowers of Adonis aestivalis. Plant Journal. 41:
478-492.
Green, B. R. and
E. Gantt. 2005. Distal and extrinsic photosystem II antennas. pp.
23-44. In: T.J. Wydrzynski and K. Satoh (eds.) Photosystem II. The
Light-Driven Water:Plastoquinone Oxidoreductase. Springer.
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