scholarly journals The Cpc1 Regulator of the Cross-Pathway Control of Amino Acid Biosynthesis Is Required for Pathogenicity of the Vascular Pathogen Verticillium longisporum

2013 ◽  
Vol 26 (11) ◽  
pp. 1312-1324 ◽  
Author(s):  
Christian Timpner ◽  
Susanna A. Braus-Stromeyer ◽  
Van Tuan Tran ◽  
Gerhard H. Braus

The plant-pathogenic fungus Verticillium longisporum is a causal agent of early senescence and ripening in cruciferous crops like Brassica napus. Verticillium wilts have become serious agricultural threats in recent decades. Verticillium species infect host plants through the roots and colonize xylem vessels of the host plant. The xylem fluid provides an environment with limited carbon sources and unbalanced amino acid supply, which requires V. longisporum to induce the cross-pathway control of amino acid biosynthesis. RNA-mediated gene silencing reduced the expression of the two CPC1 isogenes (VlCPC1-1 and VlCPC1-2) of the allodiploid V. longisporum up to 85%. VlCPC1 encodes the conserved transcription factor of the cross-pathway control. The silenced mutants were highly sensitive to amino-acid starvation, and the infected plants showed significantly fewer symptoms such as stunting or early senescence in oilseed rape plant infection assays. Consistently, deletion of single CPC1 of the haploid V. dahliae resulted in strains that are sensitive to amino-acid starvation and cause strongly reduced symptoms in the plant-host tomato (Solanum lycopersicum). The allodiploid V. longisporum and the haploid V. dahliae are the first phytopathogenic fungi that were shown to require CPC1 for infection and colonization of their respective host plants, oilseed rape and tomato.

1982 ◽  
Vol 39 (2) ◽  
pp. 169-185 ◽  
Author(s):  
Ilse B. Barthelmess

SummaryArginine-requiring mutants ofNeurospora crassawere isolated using a strain partially impaired in an enzyme of the arginine pathway (bradytroph). Among these, five strains were found which carry mutations at a new locus,cpc-1+. The recessivecpc-1alleles interfere with the cross-pathway control of amino acid biosynthetic enzymes. The enzymes studied, three of arginine and one each of histidine and lysine biosynthesis, fail to derepress under conditions which normally result in elevation of enzyme concentration, namely arginine, histidine or tryptophan limitation. Enzymes not involved in amino acid biosynthesis are still able to derepress in the presence ofcpc-1. In wild-type backgound, i.e. with the bradytroph replaced,cpc-1strains lose the original arginine-requirement.cpc-1mutations confer sensitivity of growth to 3-amino-1,2,4-triazole.


1987 ◽  
Vol 208 (1-2) ◽  
pp. 159-167 ◽  
Author(s):  
Kiyoji Nishiwaki ◽  
Naoyuki Hayashi ◽  
Shinji Irie ◽  
Dong-Hyo Chung ◽  
Satoshi Harashima ◽  
...  

2002 ◽  
Vol 99 (5) ◽  
pp. 2678-2683 ◽  
Author(s):  
B. Min ◽  
J. T. Pelaschier ◽  
D. E. Graham ◽  
D. Tumbula-Hansen ◽  
D. Soll

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