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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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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-B12B-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-B12C-1
Genre: Journal Article

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JBiolChem_291_2016_22868.pdf (Any fulltext), 3MB
 
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 Creators:
Schuebel, Felix1, Author              
Rocker, Andrea1, Author              
Edelmann, Daniel1, Author              
Schessner, Julia1, Author              
Brieke, Clara1, Author              
Meinhart, Anton1, Author              
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: enzyme inhibitor; enzyme mechanism; NAD biosynthesis; second messenger secretion; toxin; type III secretion system (T3SS)
 Abstract: 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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Language(s): eng - English
 Dates: 2016-09-012016-08-012016-09-122016-09-122016-10-01
 Publication Status: Published in print
 Pages: 20
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 291 (44) Sequence Number: - Start / End Page: 22868 - 22880 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1