Indications for the Occurrence of Nitric Oxide Synthases in Fungi and Plants and the Involvement in Photoconidiation of <i>Neurospora crassa</i>*

Ninnemann, Helga; Maier, Jutta

doi:10.1111/j.1751-1097.1996.tb02477.x

Cited by 218 publications

(156 citation statements)

References 60 publications

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“…NOS activities are present in plants and lower eukaryotes (1)(2)(3)(4)(5). Their primary structures and activities are strikingly similar to the mammalian NOSs, suggesting that NO has been important throughout evolution.…”

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confidence: 91%

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Cloning, expression, and characterization of a nitric oxide synthase protein from Deinococcus radiodurans

Adak

Bilwes

Panda

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

122

139

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We cloned, expressed, and characterized a hemeprotein from Deinococcus radiodurans (D. radiodurans NO synthase, deiNOS) whose sequence is 34% identical to the oxygenase domain of mammalian NO synthases (NOSoxys). deiNOS was dimeric, bound substrate Arg and cofactor tetrahydrobiopterin, and had a normal heme environment, despite its missing N-terminal structures that in NOSoxy bind Zn 2؉ and tetrahydrobiopterin and help form an active dimer. The deiNOS heme accepted electrons from a mammalian NOS reductase and generated NO at rates that met or exceeded NOSoxy. Activity required bound tetrahydrobiopterin or tetrahydrofolate and was linked to formation and disappearance of a typical heme-dioxy catalytic intermediate. Thus, bacterial NOS-like proteins are surprisingly similar to mammalian NOSs and broaden our perspective of NO biochemistry and function.G enes coding for NO synthases (NOSs, EC 4.14.23) are present throughout the plant and animal kingdom. NOS activities are present in plants and lower eukaryotes (1-5). Their primary structures and activities are strikingly similar to the mammalian NOSs, suggesting that NO has been important throughout evolution. All eukaryotic NOSs catalyze the NADPH-and O 2 -dependent oxidation of L-arginine (Arg) to citrulline and NO, with N-hydroxy-L-arginine (NOHA) formed as an enzyme-bound intermediate (6). Structurally, all animal NOSs are bi-domain proteins containing an N-terminal oxygenase domain (NOSoxy) that binds protoporphyrin IX (heme), 6R-tetrahydrobiopterin (H 4 B), and Arg and is linked to a C-terminal f lavoprotein domain (NOS reductase domain, NOSred) by a central calmodulin (CaM) binding sequence (7,8). NOSred bears strong sequence and functional similarity to NADPH-cytochrome P450 reductase and related electron transfer flavoproteins (9, 10), and function to transfer NADPHderived electrons to the ferric heme for O 2 activation during NO synthesis. In contrast, NOSoxy and cytochromes P450 have completely different primary, secondary, and tertiary structures, even though both enzyme families use a thiolate-ligated heme for O 2 activation (11, 12). Moreover, unlike P450s, NOSoxy must dimerize to become active (13,14). Dimerization produces functional binding sites for Arg and H 4 B and sequesters the heme catalytic center from solvent. These distinguishing features imply that NOSs evolved separately from other heme-thiolate enzymes and can so provide unique perspectives on their structure-function relationships.Although oxidative (nitrification) or reductive (denitrification) pathways for prokaryote NO biosynthesis are well established (15), there have been few reports on NOS-like proteins in bacteria (16,17). To date no prokaryotic NOS proteins have been completely sequenced, purified, or cloned. However, some have been shown to have nitrite-forming activity that depended on Arg, NADPH, and H 4 B. More recent genome sequencing of Bacillus subtilis, Deinococcus radiodurans, and other bacteria (18)(19)(20) confirm that a subset contain ORFs that code for proteins homo...

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mentioning

confidence: 91%

“…3 shows that nitrite formation by deiNOS approached V max conditions near 100 M H 4 B. Reciprocal analysis gave an apparent K m for H 4 (Fig. 3).…”

Section: Physical and Spectral Characteristics Of Deinosmentioning

confidence: 99%

Cloning, expression, and characterization of a nitric oxide synthase protein from Deinococcus radiodurans

Adak

Bilwes

Panda

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

122

139

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“…Initial evidence was based on the production of NO and L-citrulline from L-Arg by plant extracts and/or its inhibition by specific inhibitors, typically inactive substrate analogs (Cueto et al, 1996;Ninnemann and Maier, 1996;Delledonne et al, 1998;Durner et al, 1998). In a different approach, the use of antibodies against mammalian NOS enzymes detected immunoreactive proteins in different plant cell compartments (Barroso et al, 1999;Ribeiro et al, 1999).…”

Section: First Leads In the Hunt For Plant Nos Enzymesmentioning

confidence: 99%

Hunting for Plant Nitric Oxide Synthase Provides New Evidence of a Central Role for Plastids in Nitric Oxide Metabolism

et al. 2009

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Nitric oxide (NO) has emerged as a central signaling molecule in plants and animals. However, the long search for a plant NO synthase (NOS) enzyme has only encountered false leads. The first works describing a pathogen-induced NOS-like plant protein were soon retracted. New hope came from the identification of NOS1, an Arabidopsis thaliana protein with an atypical NOS activity that was found to be targeted to mitochondria in roots. Although concerns about the NO-producing activity of this protein were raised (causing the renaming of the protein to NO-associated 1), compelling data on its biological role were missing until recently. Strong evidence is now available that this protein functions as a GTPase that is actually targeted to plastids, where it might be required for ribosome function. These and other results support the argument that the defective NO production in loss-of-function mutants is an indirect effect of interfering with normal plastid functions and that plastids play an important role in regulating NO levels in plant cells.

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“…One can postulate that other signals, not yet identified, could play a role in this signalling system. As an example of such a putative signal, one can cite the involvement of nitric oxide in the light induction of conidiation in the fungus Neurospora erassa (Ninnemann & Maier 1996).…”

Section: Concluding Remarks and Perspectivesmentioning

confidence: 99%

Photomorphogenesis and phyfohormones

Kraepiel

Miginiac

1997

Plant Cell & Environment

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There are numerous reports of interactions between light and phytohormones. However, the exact nature of this interaction is not well understood. This article considers the possihle roles played in the light signal transduction chain hy four phytohormones (auxin, ahscisic acid, gihherellins and cytokinins). As the involvement of phytohormones in this signalling mechanism is controversial, the major arguments in the dehate are reported, including recently puhlished results based on genetic, biochemical and physiological approaches.

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Indications for the Occurrence of Nitric Oxide Synthases in Fungi and Plants and the Involvement in Photoconidiation of *Neurospora crassa**

Cited by 218 publications

References 60 publications

Cloning, expression, and characterization of a nitric oxide synthase protein from Deinococcus radiodurans

Cloning, expression, and characterization of a nitric oxide synthase protein from Deinococcus radiodurans

Hunting for Plant Nitric Oxide Synthase Provides New Evidence of a Central Role for Plastids in Nitric Oxide Metabolism

Photomorphogenesis and phyfohormones

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Indications for the Occurrence of Nitric Oxide Synthases in Fungi and Plants and the Involvement in Photoconidiation of Neurospora crassa*

Cited by 218 publications

References 60 publications

Cloning, expression, and characterization of a nitric oxide synthase protein from Deinococcus radiodurans

Cloning, expression, and characterization of a nitric oxide synthase protein from Deinococcus radiodurans

Hunting for Plant Nitric Oxide Synthase Provides New Evidence of a Central Role for Plastids in Nitric Oxide Metabolism

Photomorphogenesis and phyfohormones

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Indications for the Occurrence of Nitric Oxide Synthases in Fungi and Plants and the Involvement in Photoconidiation of *Neurospora crassa**