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.
| Original language | English |
|---|---|
| Pages (from-to) | 22868-22880 |
| Number of pages | 13 |
| Journal | Journal of Biological Chemistry |
| Volume | 291 |
| Issue number | 44 |
| DOIs | |
| Publication status | Published - 28 Oct 2016 |
| Externally published | Yes |
Keywords
- enzyme inhibitor
- enzyme mechanism
- NAD biosynthesis
- second messenger
- secretion
- toxin
- type III secretion system (T3SS)
Cite this
}
3′-NADP and 3′-NAADP, two metabolites formed by the bacterial type iii effector AvrRxo. / Schuebel, Felix; Rocker, Andrea; Edelmann, Daniel; Schessner, Julia; Brieke, Clara; Meinhart, Anton.
In: Journal of Biological Chemistry, Vol. 291, No. 44, 28.10.2016, p. 22868-22880.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - 3′-NADP and 3′-NAADP, two metabolites formed by the bacterial type iii effector AvrRxo
AU - Schuebel, Felix
AU - Rocker, Andrea
AU - Edelmann, Daniel
AU - Schessner, Julia
AU - Brieke, Clara
AU - Meinhart, Anton
PY - 2016/10/28
Y1 - 2016/10/28
N2 - 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.
AB - 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.
KW - enzyme inhibitor
KW - enzyme mechanism
KW - NAD biosynthesis
KW - second messenger
KW - secretion
KW - toxin
KW - type III secretion system (T3SS)
UR - http://www.scopus.com/inward/record.url?scp=84993961044&partnerID=8YFLogxK
U2 - 10.1074/jbc.M116.751297
DO - 10.1074/jbc.M116.751297
M3 - Article
VL - 291
SP - 22868
EP - 22880
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 1083-351X
IS - 44
ER -