Goethe




Institut für molekulare Biowissenschaften




Uni-Home






Prof. J. Feierabend

Retired since 2004. 1980-2004 head of the research group for  Plant Cell Physiology




Contact: Prof. Dr. J. Feierabend

Tel.: +49-69-798-24780
+49-69-798-24726
Fax: +49-69-798-24822
E-Mail: Feierabend@bio.uni-frankfurt.de

Postal adress: Botanisches Institut
Siesmayerstr. 70
Fach 213
D-60054 Frankfurt am Main
GERMANY


Research Areas

I. Photo-oxidative Stress
II. Cold-Acclimation
III. Cellular signal transduction in senescing leaves and under cold stress


I. Photo-oxidative Stress: biochemical and molecular mechanisms and strategies of stress tolerance

Subject Area: In green plants pigments and reactions of photosynthesis may mediate the production of reactive oxygen species (ROS) in light. ROS production is enhanced by CO2-deficiency and by various stress conditions leading to over-excitation of photosynthetic electron transport because NADPH cannot be sufficiently consumed by assimilatory reactions. ROS may damage membranes, pigments, proteins and nucleic acids. Finally "oxidative stress" may become lethal to plants. Therefore plants have evolved numerous protective mechanisms for the avoidance or removal of ROS ("antioxidants").

In spite of the presence of various protective systems certain proteins engaged in photosynthetic metabolism can usually not fully escape oxidative inactivation by light. The reaction center protein D1 of photosystem II (PSII) and the enzyme catalase which detoxifies the H 2O2 produced during photorespiration in the peroxisomes are inactivated and degraded in light and have to be replaced by de novo synthesis (repair). Their turnover increases with light intensity. Therefore, repair activities must be controlled and continuously adjusted to changing light conditions. De novo synthesis in order to repair both the D1 protein and catalase is regulated at the level of translation. Analysis of translational mechanisms controlling catalase synthesis represent a main topic of the present research of our group. When the capacity for repair is unsufficient, photoinhibition of PSII and a loss of catalase are induced in light. The loss of catalase further weakens antioxidative protection. As a consequence, photooxidative injury is enhanced and plant growth and yield decline under stress conditions, such as high light intensity, heat, low temperature, salt or exposure to pollutants.

However, several plants are able to acclimate to extreme environmental conditions and to avoid photooxidative injury. In order to analyze machanisms of stress tolerance, cold-hardened winter cereals (grown at low temperature) and alpine high mountain plants are investigated that have to survive very extreme unfavorable environmental conditions with a very short growing season. In an alpine high mountain plant (Homogyne alpina L.) a catalase of higher stability was found and its cDNA was cloned. This catalase cDNA is heterologously expressed in insect cell cultures in order to identify structures and sequences that are responsible for stability or light-sensitivity of catalases.



II. Cold-Acclimation

Subject area: Numerous plants are able to acclimate to low temperatures. Plants are protected against cold injury by the concerted expression of various cold-specific genes and the biochemical and metabolic changes resulting from the cooperation of their products. These include both proteins or enzymes that are engaged in protection against cold injuries and regulatory factors controlling the expression of such proteins.


III. Cellular Signal Transduction in Senescing Leaves and under Cold Stress (PD Dr. Th. Berberich)

Subject Area: In higher plants environmental and developmental changes lead to differential gene expression. Specific cellular signalling pathways determine which genes are switched on or off. Components like transcription factors, calcium ions and protein kinases are part of the signalling cascades. We have characterized factors which play a role in the cellular signalling in low-temperature stress and senescence in maize and tobacco. The function of these regulatory proteins will be examined in detail and further signalling molecules will be identified. Modern techniques in the field of molecular biology like DNA-protein and protein-protein interaction are employed. This research project is in close cooperation with Prof. Kusano at Tohoku-University in Sendai, Japan.


Publications

Berberich, Th. and J. Feierabend: The onset of 70S chloroplast ribosome formation is determined by an early heat-sensitive stage in the ontogeny of rye leaves. Plant Cell Physiol. 35, 907-916 (1994).

Schmidt, M., I. Svendsen, and J. Feierabend: Analysis of the primary structure of the chloroplast isozyme of triosephosphate isomerase from rye leaves by protein and cDNA sequencing indicates a eukaryotic origin of its gene. Biochim. Biophys. Acta 1261, 257-264 (1995).

Kusano, T., Berberich, T., Harada, M., Suzuki, N. and Sugawara, K.: A maize DNA-binding factor with a bZIP motif is induced by low-temperature. Mol. Gen. Genet. 248, 507-517 (1995)

Berberich, T., Sugawara, K., Harada, M. and Kusano, T.: Molecular cloning, characterization and expression of an elongation factor 1 a gene in maize. Plant Mol. Biol. 29, 611-615 (1995)

Feierabend, J. and Dehne, S.: Fate of the porphyrin cofactors during the light-dependent turnover of catalase and of the photosystem II reaction center protein D1 in mature rye leaves. Planta 198, 413-422 (1996).

Schmitz, G., Schmidt, M. and Feierabend, J.: Characterization of a plastid-specific HSP90 homologue: Identification of a cDNA sequence, phylogenetic descendence and analysis of its mRNA and protein expression. Plant Mol. Biol. 30, 479-492 (1996).

Streb, P. and Feierabend, J.: Oxidative stress responses accompanying photoinactivation of catalase in NaCl-treated rye leaves. Botan. Acta 109, 125-132 (1996).

Feierabend, J., Streb, P., Schmidt, M., Dehne, S. and Shang, W.: Expression of catalase and its relation to light stress and stress tolerance. In: Physical Stresses in Plants. Genes and their Products for Tolerance. (Eds. S. Grillo & A. Leone), pp. 223-234, Springer, Berlin, Heidelberg, 1996.

Streb, P., Schaub, H. and Feierabend, J.: Latent oxidative stress responses of ozone-fumigated cucumber plants are enhanced by simultaneous cold exposures. Z. Naturforsch. 51c, 355-362 (1996).

Schmitz, G., Schmidt, M. and Feierabend, J.: Comparison of the expression of a plastidic chaperonin 60 in different plant tissues and under photosynthetic and non-photosynthetic conditions. Planta 200, 326-334 (1996)

Berberich, T. and Kusano, T.: Cycloheximide induces a subset of low temperature-inducible genes in maize. Mol. Gen. Genet. 254, 275-283 (1997).

Streb, P., Tel-Or, E. and Feierabend, J.: Light stress effects and antioxidative protection in two desert plants. Funct. Ecol. 11, 416-424 (1997).

Streb, P., Feierabend, J. and Bligny, R.: Resistance to photoinhibition of photosystem II and catalase and antioxidative protection in high mountain plants. Plant Cell Environ. 20, 1030-1040 (1997).

Shang, W. and Feierabend, J.: Slow turnover of the D1 reaction center protein of photosystem II in leaves of high mountain plants. FEBS Lett. 425, 97-100 (1998)

Jagtap, V., Bhargava, S., Streb, P. and Feierabend, J.: Comparative effect of water, heat, and light stresses on photosynthetic reactions in Sorghum bicolor (L.) Moench. J. Exp. Bot. 49, 1715-1721 (1998)

Berberich, Th., Uebeler, M. and Feierabend, J.: Cloning of a cDNA encoding a thioredoxin peroxidase homolog from winter rye (Accession no. AF076920). (PGR 98-167). Plant Physiol. 118, 711 (1998)

Streb, P., Shang, W., Feierabend, J. and Bligny, R.: Divergent strategies of photoprotection in high-mountain plants. Planta 207, 313-324 (1998)

Kusano, T., Sugawara, K., Harada, M. and Berberich, Th.: Molecular cloning and partial characterization of a tobacco cDNA encoding a small bZIP protein. Biochim. Biophys. Acta 1395, 171-175 (1998)

Berberich, Th., Harada, M., Sugawara, K., Kodama, H., Iba, K. and Kusano, T.: Two maize genes encoding w -3 fatty acid desaturase and their differential expression to temperature. Plant Mol. Biol. 36, 297-306 (1998)

Shang W., Feierabend J.: Dependence of catalase photoinactivation in rye leaves on light intensity and quality and characterization of a chloroplast-mediated inactivation in red light. Photosynthesis Res. 59, 201-213 (1999)

Berberich T., Sano H., Kusano T.: Involvement of a MAP kinase, ZmMPK5, in senescence and recovery from low-temperature stress in maize. Mol. Gen. Genet. 262, 534-542 (1999)

Streb P., Shang W., and Feierabend, J.: Resistance of cold-hardened winter rye leaves (Secale cereale L.) to photo-oxidative stress. Plant, Cell Environ. 22, 1211-1223 (1999)

Streb P., and Feierabend, J.: Significance of antioxidants and electron sinks for the cold-hardening-induced resistance of winter rye leaves to photo-oxidative stress. Plant Cell Environ. 22,1225-1237 (1999)

Schmidt, M. and Feierabend, J.: Characterization of cDNA nucleotide sequences encoding two differentially expressed catalase isozyme polypeptides from winter rye (Secale cereale L.) (Acdession nos. Z54143, Z99634 and AJ251894). (PGR 00-032). Plant Physiol. 122, 1457 (2000)

Schäfer, L. and Feierabend, J.: Photoinactivation and protection of glycolate oxidase in vitro and in leaves. Z. Naturforsch. 55c, 361-372 (2000)

Ohba, H., Steward, N., Kawasaki, S., Berberich, T., Ikeda, Y., Koizumi, N., Kusano, T., Sano, H.: Diverse response of rice and maize genes encoding homologs of WPK4, an SNF1-related kinase from wheat, to light, nutrients, low temperature and cytokinins. Mol Gen Genet 263, 359-366 (2000)

Berberich, T., Uebeler, M. and Feierabend, J.: cDNA cloning of cytoplasmic ribosomal protein S7 of winter rye (Secale cereale) and its expression in low-temperature treated leaves. Biochim. Biophys. Acta, 1492 276-279 (2000)

Schmidt, M., Dehne, S. and Feierabend, J.: Regulation of catalase synthesis during its light-induced turnover in leaves. PS 2001 Proceedings: 12th International Congress on Photosynthesis. CSIRO Publishing: Melbourne, Australia 2001, Available at: http://www.publish.csiro.au/2001

Yang, S.H., Berberich, T., Sano, H. and Kusano, T.: Specific association of transcripts of tbzF and tbz17, tobacco genes encoding bZIP-type transcriptional activators, with guard cells of senescing leaves and/or flowers. Plant Physiol. 127, 23-32 (2001)

Schmidt, M., Dehne, S. and Feierabend, J.: Posttrancriptional mechanisms control catalase synthesis during its light-induced turnover in rye leaves through the availability of the hemin cofactor and reversible changes of the translation efficiency of the mRNA. Plant J. 31 (5), 601- 613 (2002)

Shang, W., Schmidt, M. and Feierabend, J.: Increased capacity for synthesis of the D1 protein and of catalase at low temperature in leaves of cold-hardened winter rye (Secale cereale L.) Planta, 216 (5), 865-873 (2003)

Crecelius, F., Streb, P. and Feierabend, J.: Malate metabolism and reactions of oxidoreduction in cold-hardened winter rye (Secale cereale L.) leaves J Exp Bot, 54 (384), 1075-1083 (2003)


In,O., Berberich, Th., Romdhane, S. and Feierabend, J.: Changes in gene expression during dehardening of cold-hardened winter rye (Secale cereale L.) leaves and potential role of a peptide methionine sulfoxide reductase in cold-acclimation. Planta 220, 941-950 (2005)

Feierabend, J.: Catalases in plants: molecular and functional properties and role in stress defence. In: Smirnoff, N. (ed.) Antioxidants and reactive oxygen species in plants. Blackwell Publ., Oxford, pp. 101-140 (2005)

Engel, N., Schmidt, M., Lütz, C. and Feierabend, J.: Molecular identification, heterologous expression and properties of light-insensitive plant catalases. Plant Cell Envir, 29, 593-607 (2006)

Schmidt, M., Grief, J. and Feierabend, J.:  Mode of translational activation of the Catalase (Cat1) mRNA of rye leaves (Secale cereale L.) and its control through blue light and reactive oxygen. Planta, 223, 835-846 (2006)

 


M.Schmidt , 02-Oct-06