This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Maheswaran, M.
Right arrow Articles by Forchhammer, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Maheswaran, M.
Right arrow Articles by Forchhammer, K.

 Previous Article  |  Next Article 

Journal of Bacteriology, April 2006, p. 2730-2734, Vol. 188, No. 7
0021-9193/06/$08.00+0     doi:10.1128/JB.188.7.2730-2734.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

PII-Regulated Arginine Synthesis Controls Accumulation of Cyanophycin in Synechocystis sp. Strain PCC 6803

Mani Maheswaran,1 Karl Ziegler,2 Wolfgang Lockau,2 Martin Hagemann,3 and Karl Forchhammer1*

Institut für Mikrobiologie und Molekularbiologie, Justus-Liebig Universität Giessen, Heinrich-Buff-Ring 26-32, D-35392 Giessen, Germany,1 Institut für Biologie, Humboldt-Universität zu Berlin, Chausseestr. 117, D-10115 Berlin, Germany,2 Abteilung Pflanzenphysiologie, Universität Rostock, Albert-Einstein-Str. 3, D-18051 Rostock, Germany3

Received 1 December 2005/ Accepted 20 January 2006

Cyanophycin (multi-L-arginyl-poly-L-aspartic acid) is a nitrogen storage polymer found in most cyanobacteria and some heterotrophic bacteria. The cyanobacterium Synechocystis sp. strain PCC 6803 accumulates cyanophycin following a transition from nitrogen-limited to nitrogen-excess conditions. Here we show that the accumulation of cyanophycin depends on the activation of the key enzyme of arginine biosynthesis, N-acetyl-L-glutamate kinase, by signal transduction protein PII.

* Corresponding author. Mailing address: Institut für Mikrobiologie und Molekularbiologie, Justus-Liebig Universität Giessen, Heinrich-Buff-Ring 26-32, D-35392 Giessen, Germany. Phone: 0049-641-9935545. Fax: 0049-641-9935549. E-mail: Karl.Forchhammer{at}mikro.bio.uni-giessen.de.

Journal of Bacteriology, April 2006, p. 2730-2734, Vol. 188, No. 7
0021-9193/06/$08.00+0     doi:10.1128/JB.188.7.2730-2734.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Paz-Yepes, J., Flores, E., Herrero, A. (2009). Expression and Mutational Analysis of the glnB Genomic Region in the Heterocyst-Forming Cyanobacterium Anabaena sp. Strain PCC 7120. J. Bacteriol. 191: 2353-2361 [Abstract] [Full Text]  
  • Schriek, S., Kahmann, U., Staiger, D., Pistorius, E. K., Michel, K.-P. (2009). Detection of an L-amino acid dehydrogenase activity in Synechocystis sp. PCC 6803. J Exp Bot 60: 1035-1046 [Abstract] [Full Text]  
  • Llacer, J. L., Contreras, A., Forchhammer, K., Marco-Marin, C., Gil-Ortiz, F., Maldonado, R., Fita, I., Rubio, V. (2007). The crystal structure of the complex of PII and acetylglutamate kinase reveals how PII controls the storage of nitrogen as arginine. Proc. Natl. Acad. Sci. USA 104: 17644-17649 [Abstract] [Full Text]  
  • Takatani, N., Kobayashi, M., Maeda, S.-i., Omata, T. (2006). Regulation of Nitrate Reductase by Non-Modifiable Derivatives of PII in the Cells of Synechococcus elongatus Strain PCC 7942. Plant Cell Physiol 47: 1182-1186 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»