Hans J. Bohnert. Professor, Departments of Biochemistry and Plant
Sciences and Molecular and Cellular Biology. Ph.D., Heidelberg University.
Plant gene expression in response to
environmental stress; multigene transfer technology; biochemical pathway
engineering in transgenic plants; expression profiling by ESTs and
microarrays; sodium long-distance transport.
- Office: Biological Sciences West, #540 (621-7961)
- Laboratory: Biological Sciences West, #513 (621-7982)
- e-mail: hbohnert@biosci.arizona.edu
Chloroplast/cytosol interaction, plastid evolution, plant gene expression
in response to environmental stress, enzyme engineering in transgenic plants.
Research in the laboratory is directed towards the dissection of plant
metabolism using tools of molecular biology. Areas of emphasis are, at present,
(i) the analysis of gene expression responses to environmental stresses,
mainly salt stress; (ii) the analysis of promoter elements of environmentally-regulated
and developmentally-regulated genes; (iii) plastid-nucleus interaction,
and (iv) the study of transgenic plants over-expressing foreign genes.
The common ice plant (Mesembryanthemum crystallinum) has been developed
into a model to study environmental stress under aspects of genetics, physiology
and biochemistry. The plant has a small genome; its responses to environmental
stress (salt, drought, low temperature), and responses to hormones are well
defined physiologically (C3 to CAM switching) and biochemically (carbohydrate
and proline accumulation); a number of stress-induced genes have been obtained;
and morphological markers of stress-enhanced development have been established.
Analysis of environmentally induced changes in gene expression progresses
at present from the analysis of promoter elements important for the stress-enhanced
induction of CAM to the analysis of genes in metabolic pathways not related
to CAM.
In the cyanelles of Cyanophora paradoxa a different integration of cytosol
and plastid compartments is realized compared to that in higher plants.
Cyanelles are as dependent as are chloroplasts on nucleus-encoded transported
proteins, however, the cyanelles have retained genes that are nuclear in
higher plants, such as nadA (quinolate synthetase), crtE (pre-phytoene pyrophosphate
dehydrogenase). Cyanelles also appear to maintain a protein export machinery.
Such features make these organelles ideal study objects for studying plastid
acquisition, protein translocation and compartmental integration.
DeRocher EJ, Bohnert HJ (1993) Development and environmental stress employ
different mechanisms in the expression of a plant gene family. Plant Cell
5:1611-25.
Tarczynski M, RG Jensen, HJ Bohnert (1993) Stress protection of transgenic
tobacco by production of the osmolyte mannitol. Science 259:508-10.
Thomas JC, A Smigocki, HJ Bohnert (1995) Light-induced expression of Ipt
from Agrobacterium tumefaciens results in cytokinin production and osmotic
stress symptoms in transgenic tobacco. Plant Mol. Biol. 27:225-35.
Thomas JC, DG Adams, C Nessler, JK Brown, HJ Bohnert (1995) Reduced whitefly
(Besmisia tabaci) reproduction on transgenic tobacco expressing tryptophan
decarboxylase. Plant Physiol. 109:in press.
Yamada S, M Katsuhara, W Kelly, CB Michalowski, HJ Bohnert (1995) A family
of transcripts encoding MIP-homologues - Tissue specificity of expression
under salt stress in Mesembryanthemum crystallinum. Plant Cell 7(8):1129-1142.
Bohnert HJ, D Nelson, RG Jensen (1995) Adaptations to environmental stress.
Plant Cell, in press (8/95) 7:1099-1111.
Stirewalt V.L., C.B. Michalowski, W. Loffelhardt, H.J. Bohnert, and D.A.
Bryant. Nucleotide Sequence of the Cyanelle Genome from Cyanophora paradoxa.
Plant Molecular Biology Reporter vol. 13(4) 1995. pp. 342-347.
J.C. Thomas, D.G. Adams, V.D. Keppenne, C.C. Wasmann, J.K. Brown, M.R. Kanost,
and H.J. Bohnert. Manduca sexta encoded protease inhibitors expressed in
Nicotiana tabacum provide protection against insects. Plant Physiol. Biochem.
1995, 33(5), 611-614.
G. Rammesmayer, H. Pichorner, P. Adams, R.G. Jensen, and H.J. Bohnert. Characterization
of IMT1, myo-Inositol O-methyltransferase, from Mesembryanthemum crystallinum1.
Archives of Biochemistry and Biophysics, Vol. 322, No. 1, Sept. 10, pp.
183-188, 1995.