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Functional analysis of the members of the sulfurtransferase/rhodanese multi protein family in Arabidopsis

Subject Area Evolution and Systematics of Plants and Fungi
Term from 1999 to 2009
Project identifier Deutsche Forschungsgemeinschaft (DFG) - Project number 5168838
 
Final Report Year 2010

Final Report Abstract

Our research aims at the elucidation of the properties and functional in vivo relevance of the now 20 members of the heterogeneous sulfurtransferase multi protein family in Arabidopsis thaliana (AtStr). In Oryza sativa L. 24 Str proteins have been identified and grouped into five groups according to their sequence homology. To almost all Oryza Str a homologue in Arabidopsis could be identified despite of the 3x larger genome and 1.5x more genes in Oryza. Mainly in the group containing two-domain Str there are more Oryza Str. Heterologously expressed and purified OsStr22 shows very low enzyme activity whereas the AtStrl homologue from Brassica napus (BnStrl) shows very high enzyme activity with mercaptopyruvate and thiosulfate. BnStrl mRNA was highly induced by infection with bacterial pathogens in hydroponic cultures of Brassica napus. There are a number of Str T- DNA insertion mutants available. Additionally, we produced RNAi plants using the AtStrl, the AtStrl C-terminal domain and AtStrl 5 sequences in the Gateway system. The RNAi plants did not grow further after germination indicating a severe loss of function although we tried different gentle growth conditions. Therefore Arabidopsis plant cell cultures were transformed with the respective RNAi constructs. The transformed unstressed cells are viable and will be used for further stress experiments. BiFC analysis of thioredoxins and Str indicate a specific interaction of members of these protein families. Therefore Str might play a role in the control of the redox homeostasis in the different subcellular compartments.

Publications

  • (2009) Reduced sulfur in the plant cell - enzymatic formation and functional roles. In: Sulfur Metabolism in Higher Plants. Sirko, A. et al. (eds), Backhuys Publishers, Leiden, The Netherlands, pp. 217-219
    Papenbrock J, Bartels A, Hartmann F, Hartmann J, Triulzi T
  • (2010) Latest news about the sulfurtransferase protein family of higher plants. Amino Acids. 2010 Feb 5. [Epub ahead of print]
    Papenbrock J, Guretzki S, Henne M
  • (2010) Mobilization of sulfane sulfur from cysteine desulfurases to the Azotobacter vinelandii sulfurtransferase RhdA. Amino Acids. 2010 Mar 7. [Epub ahead of print]
    Cartini F, Remelli W, Dos Santos PC, Papenbrock J, Pagani S, Forlani F
 
 

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