1. A singular nitric oxide synthase with a globin domain found in Synechococcus PCC 7335 mobilizes N from arginine to nitrate
- Author
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Lorenzo Lamattina, Noelia Foresi, Fiorella Del Castello, and Natalia Correa-Aragunde
- Subjects
0106 biological sciences ,0301 basic medicine ,Oxygenase ,globin domain ,Arginine ,Protein domain ,lcsh:Medicine ,macromolecular substances ,Reductase ,01 natural sciences ,Article ,purl.org/becyt/ford/1 [https] ,Ciencias Biológicas ,03 medical and health sciences ,chemistry.chemical_compound ,Biología Celular, Microbiología ,Bacterial Proteins ,Protein Domains ,Escherichia coli ,Citrulline ,Globin ,lcsh:Science ,purl.org/becyt/ford/1.6 [https] ,Synechococcus ,Nitrates ,Multidisciplinary ,biology ,nitric oxide synthase ,lcsh:R ,Phycoerythrin ,biology.organism_classification ,Nitric oxide synthase ,Synechococcus PCC 7335 ,NG-Nitroarginine Methyl Ester ,030104 developmental biology ,Biochemistry ,chemistry ,biology.protein ,bacteria ,lcsh:Q ,Nitric Oxide Synthase ,Genetic Engineering ,CIENCIAS NATURALES Y EXACTAS ,010606 plant biology & botany - Abstract
The enzyme nitric oxide synthase (NOS) oxidizes L-arginine to NO and citrulline. In this work, we characterise the NOS from the cyanobacteria Synechococcus PCC 7335 (SyNOS). SyNOS possesses a canonical mammalian NOS architecture consisting of oxygenase and reductase domains. In addition, SyNOS possesses an unusual globin domain at the N-terminus. Recombinant SyNOS expressed in bacteria is active, and its activity is suppressed by the NOS inhibitor L-NAME. SyNOS allows E. coli to grow in minimum media containing L-arginine as the sole N source, and has a higher growth rate during N deficiency. SyNOS is expressed in Synechococcus PCC 7335 where NO generation is dependent on L-arginine concentration. The growth of Synechococcus is dramatically inhibited by L-NAME, suggesting that SyNOS is essential for this cyanobacterium. Addition of arginine in Synechococcus increases the phycoerythrin content, an N reservoir. The role of the novel globin domain in SyNOS is discussed as an evolutionary advantage, conferring new functional capabilities for N metabolism. Fil: Correa Aragunde, Maria Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina Fil: Foresi, Noelia Pamela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina Fil: del Castello, Fiorella Paola. Universidad Nacional de Mar del Plata; Argentina Fil: Lamattina, Lorenzo. Universidad Nacional de Mar del Plata; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
- Published
- 2018