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Structural modeling and environmental regulation of arginine decarboxylase in Synechocystis sp. PCC 6803

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Abstract

Arginine decarboxylase (ADC) is the first enzyme in the alternative route to putrescine in the polyamine biosynthesis pathway in bacteria and plants. In this study, we have focused on the effects of various types of short-term stresses on the transcript amount and specific activity of Synechocystis sp. PCC 6803 ADC. Our results reveal that the steady-state transcript accumulation and enzyme activity are not connected in a simple manner, since only photoheterotrophy and synergistic salt and high-light stress affected both parameters similarly. Changes in the steady-state ADC mRNA accumulation under the other short-term stress conditions studied had only a small impact on enzyme activity, suggesting post-translational regulation. Based on structural modeling, Synechocystis ADCs have a putative extra domain, which might be involved in the post-translational regulation of ADC activity in Synechocystis. In addition, two symmetric inter-subunit disulfide bonds seem to stabilize the dimeric structure of ADCs. There are two genes coding for ADC and agmatinase, another polyamine pathway enzyme, in Synechocystis genome, while the genes coding for ornithine decarboxylase and for some other enzymes in the polyamine pathway were not identified with homology searches.

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Abbreviations

ADC:

Arginine decarboxylase

AIH:

Agmatine iminohydrolase

DapDC:

Diaminopimelate decarboxylase

DCMU:

3-(3′,4′-Dichlorphenyl)-1,1-dimethylurea

DFMO:

DL-α-difluoromethylornithine

NCPAH:

N-carbamoylputrescine amidohydrolase

ODC:

Ornithine decarboxylase

PDB:

Protein data bank

PLP:

Pyridoxal-5′-phosphate

RT-PCR:

Reverse transcription polymerase chain reaction

SAM:

S-adenosylmethionine

SAMDC:

S-adenosylmethionine decarboxylase

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Acknowledgments

The authors thank Professor Mark Johnson for the excellent facilities provided at the Structural Bioinformatics Laboratory of the Department of Biochemistry and Pharmacy, Åbo Akademi University. This work was supported by the Center for International Mobility (CIMO), Finland to S. Jantaro and the National Graduate School of Informational and Structural Biology, Svenska Kulturfonden and the Magnus Ehrnrooth Foundation to H. Kidron and by the Academy of Finland to T. Salminen and P. Mäenpää.

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Authors and Affiliations

  1. Department of Biology, Laboratory of Plant Physiology and Molecular Biology, University of Turku, 20014, Turku, Finland

    Saowarath Jantaro, Paula Mulo & Pirkko Mäenpää

  2. Department of Biochemistry and Pharmacy, Åbo Akademi University, 20520, Turku, Finland

    Heidi Kidron, Delphine Chesnel & Tiina Salminen

  3. Department of Biochemistry, Faculty of Science, Chulalongkorn University, 10330, Bangkok, Thailand

    Saowarath Jantaro & Aran Incharoensakdi

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  1. Saowarath Jantaro
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  2. Heidi Kidron
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  5. Paula Mulo
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Correspondence to Pirkko Mäenpää.

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Saowarath Jantaro, Heidi Kidron, Tiina Salminen and Pirkko Mäenpää have contributed equally to this work

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Jantaro, S., Kidron, H., Chesnel, D. et al. Structural modeling and environmental regulation of arginine decarboxylase in Synechocystis sp. PCC 6803. Arch Microbiol 184, 397–406 (2006). https://doi.org/10.1007/s00203-005-0064-6

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  • DOI: https://doi.org/10.1007/s00203-005-0064-6

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