Regulatory sequences of Arabidopsis drive reporter gene expression in nematode feeding structures.
In the quest for plant regulatory sequences capable of driving nematode-triggered effector gene expression in feeding structures, we show that promoter tagging is a valuable tool. A large collection of transgenic Arabidopsis plants was generated. They were transformed with a beta-glucuronidase gene functioning as a promoter tag. Three T-DNA constructs, pGV1047, p delta gusBin19, and pMOG553, were used. Early responses to nematode invasion were of primary interest. Six lines exhibiting beta-glucuronidase activity in syncytia induced by the beet cyst nematode were studied. Reporter gene activation was also identified in galls induced by root knot and ectoparasitic nematodes. Time-course studies revealed that all six tags were differentially activated during the development of the feeding structure. T-DNA-flanking regions responsible for the observed responses after nematode infection were isolated and characterized for promoter activity.
Barthels
N
N
Department of Genetics, Flanders Interuniversity Institute for Biotechnology (VIB), Universiteit Gent, Belgium.
van der Lee
F M
FM
Klap
J
J
Goddijn
O J
OJ
Karimi
M
M
Puzio
P
P
Grundler
F M
FM
Ohl
S A
SA
Lindsey
K
K
Robertson
L
L
Robertson
W M
WM
Van Montagu
M
M
Gheysen
G
G
Sijmons
P C
PC
D000818:Animals; D017360:Arabidopsis / Q000235:genetics* / Q000469:parasitology*; D001483:Base Sequence; D017931:DNA Primers / Q000235:genetics; D004269:DNA, Bacterial / Q000235:genetics; D018506:Gene Expression Regulation, Plant; D017343:Genes, Plant; D005809:Genes, Regulator; D017930:Genes, Reporter; D005822:Genetic Vectors; D005966:Glucuronidase / Q000235:genetics; D009348:Nematoda / Q000472:pathogenicity*; D010935:Plant Diseases / Q000235:genetics / Q000469:parasitology; D030821:Plants, Genetically Modified; D016133:Polymerase Chain Reaction; D011401:Promoter Regions, Genetic; D015533:Transcriptional Activation
D017931:DNA Primers; D004269:DNA, Bacterial; C036483:T-DNA; D005966:Glucuronidase