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Mobilization of sulfane sulfur from cysteine desulfurases to the Azotobacter vinelandii sulfurtransferase RhdA

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Abstract

Mobilization of the l-cysteine sulfur for the persulfuration of the rhodanese of Azotobacter vinelandii, RhdA, can be mediated by the A. vinelandii cysteine desulfurases, IscS and NifS. The amount of cysteine was higher in mutant strains lacking rhdA (MV474) than in wild type. The diazotrophic growth of MV474 was impaired. Taking into account the functional results about rhodanese-like proteins and RhdA itself, it is suggested that RhdA-dependent modulation of l-cysteine levels must deal with a redox-related process.

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Acknowledgments

Mobility of researchers between Italy and Germany was sponsored by Vigoni project n. 0815171 (2009-2010; Ateneo Italo-Tedesco, Deutscher Akademischer Austausch Dienst) to FF and JP. FF was funded by “Fondo interno ricerca scientifica e tecnologica” (2005, 2006; Università degli Studi di Milano). We thank Eleonora di Paolo, Marco Pavoni and Dr. Aristodemo Carpen for skillful technical assistance. We also thank Prof. L.E. Vickery for providing E. coli IscSC328A and Prof. D.R. Dean and Dr. D. Johnson for providing pDB943 and pDB551.

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Authors and Affiliations

  1. Dipartimento di Scienze Molecolari Agroalimentari, Università degli Studi di Milano, Via Celoria 2, 20133, Milan, Italy

    Francesca Cartini, William Remelli, Silvia Pagani & Fabio Forlani

  2. Department of Chemistry, Wake Forest University, Winston-Salem, NC, 27109, USA

    Patricia C. Dos Santos

  3. Institute for Botany, Leibniz University Hannover, Herrenhäuserstrasse 2, Hannover, Germany

    Jutta Papenbrock

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  1. Francesca Cartini
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  2. William Remelli
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  3. Patricia C. Dos Santos
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  4. Jutta Papenbrock
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  5. Silvia Pagani
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  6. Fabio Forlani
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Correspondence to Fabio Forlani.

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F. Cartini and W. Remelli contributed equally to this work.

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Cartini, F., Remelli, W., Dos Santos, P.C. et al. Mobilization of sulfane sulfur from cysteine desulfurases to the Azotobacter vinelandii sulfurtransferase RhdA. Amino Acids 41, 141–150 (2011). https://doi.org/10.1007/s00726-010-0529-z

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  • DOI: https://doi.org/10.1007/s00726-010-0529-z

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