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  3'-Nadp and 3'-Naadp - two metabolites formed by the bacterial type III effector AvrRxo1

Schuebel, F., Rocker, A., Edelmann, D., Schessner, J., Brieke, C., & Meinhart, A. (2016). 3'-Nadp and 3'-Naadp - two metabolites formed by the bacterial type III effector AvrRxo1. The Journal of Biological Chemistry, 291(44), 22868-22880. doi:10.1074/jbc.M116.751297.

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 Urheber:
Schuebel, Felix1, Autor           
Rocker, Andrea1, Autor           
Edelmann, Daniel1, Autor           
Schessner, Julia1, Autor           
Brieke, Clara1, Autor           
Meinhart, Anton1, Autor           
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Schlagwörter: enzyme inhibitor; enzyme mechanism; NAD biosynthesis; second messenger secretion; toxin; type III secretion system (T3SS)
 Zusammenfassung: An arsenal of effector proteins is injected by bacterial pathogens into the host cell or its vicinity to increase virulence. The commonly used top-down approaches inferring the toxic mechanism of individual effector proteins from the host's phenotype are often impeded by multiple targets of different effectors as well as by their pleiotropic effects. Here we describe our bottom-up approach, showing that the bacterial type III effector AvrRxo1 of plant pathogens is an authentic phosphotransferase that produces two novel metabolites by phosphorylating nicotinamide/nicotinic acid adenine dinucleotide at the adenosine 3′-hydroxyl group. Both products of AvrRxo1, 3′-NADP and 3′-nicotinic acid adenine dinucleotide phosphate (3′-NAADP), are substantially different from the ubiquitous co-enzyme 2′-NADP and the calcium mobilizer 2′-NAADP. Interestingly, 3′-NADP and 3′-NAADP have previously been used as inhibitors or signaling molecules but were regarded as “artificial” compounds so far. Our findings now necessitate a shift in thinking about the biological importance of 3′-phosphorylated NAD derivatives.

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Sprache(n): eng - English
 Datum: 2016-09-012016-08-012016-09-122016-09-122016-10-01
 Publikationsstatus: Erschienen
 Seiten: 20
 Ort, Verlag, Ausgabe: -
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 Art der Begutachtung: Expertenbegutachtung
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Titel: The Journal of Biological Chemistry
  Andere : JBC
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Seiten: - Band / Heft: 291 (44) Artikelnummer: - Start- / Endseite: 22868 - 22880 Identifikator: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1