scholarly journals Infection Structure-Specific Expression of  -1,3-Glucan Synthase Is Essential for Pathogenicity of Colletotrichum graminicola and Evasion of  -Glucan-Triggered Immunity in Maize

2013 ◽  
Vol 25 (6) ◽  
pp. 2356-2378 ◽  
Author(s):  
E. Oliveira-Garcia ◽  
H. B. Deising
Keyword(s):  
Colletotrichum Graminicola ◽  
Specific Expression ◽  
Glucan Synthase ◽  
Infection Structure

scholarly journals Infection Structure-Specific Reductive Iron Assimilation Is Required for Cell Wall Integrity and Full Virulence of the Maize Pathogen Colletotrichum graminicola

2013 ◽  
Vol 26 (6) ◽  
pp. 695-708 ◽  
Author(s):  
Emad Albarouki ◽  
Holger B. Deising
Keyword(s):  
Cell Wall ◽  
Fluorescent Protein ◽  
Transcript Abundance ◽  
Colletotrichum Graminicola ◽  
Specific Expression ◽  
Infection Structure ◽  
Double Deletion ◽  
Iron Assimilation ◽  
Essential Components ◽  
Green Fluorescent

Ferroxidases are essential components of the high-affinity reductive iron assimilation pathway in fungi. Two ferroxidase genes, FET3-1 and FET3-2, have been identified in the genome of the maize anthracnose fungus Colletotrichum graminicola. Complementation of growth defects of the ferroxidase-deficient Saccharomyces cerevisiae strain Δfet3fet4 showed that both Fet3-1 and Fet3-2 of C. graminicola represent functional ferroxidases. Expression of enhanced green fluorescent protein fusions in yeast and C. graminicola indicated that both ferroxidase proteins localize to the plasma membrane. Transcript abundance of FET3-1 increased dramatically under iron-limiting conditions but those of FET3-2 were hardly detectable. Δfet3-1 and Δfet3-2 single as well as Δfet3-1/2 double-deletion strains were generated. Under iron-sufficient or deficient conditions, vegetative growth rates of these strains did not significantly differ from that of the wild type but Δfet3-1 and Δfet3-1/2 strains showed increased sensitivity to reactive oxygen species. Furthermore, under iron-limiting conditions, appressoria of Δfet3-1 and Δfet3-1/2 strains showed significantly reduced transcript abundance of a class V chitin synthase and exhibited severe cell wall defects. Infection assays on intact and wounded maize leaves, quantitative data of infection structure differentiation, and infection stage-specific expression of FET3-1 showed that reductive iron assimilation is required for appressorial penetration, biotrophic development, and full virulence.

scholarly journals Neurospora crassa 1,3-α-glucan synthase, AGS-1, is required for cell wall biosynthesis during macroconidia development

Microbiology ◽  
2014 ◽  
Vol 160 (8) ◽  
pp. 1618-1627 ◽  
Author(s):  
Ci Fu ◽  
Asuma Tanaka ◽  
Stephen J. Free
Keyword(s):  
Cell Wall ◽  
Neurospora Crassa ◽  
Fluorescent Protein ◽  
Regulatory Elements ◽  
Specific Expression ◽  
Glucan Synthase ◽  
Aerial Hyphae ◽  
Cell Type Specific Expression ◽  
Direct Cell ◽  
Cell Type Specific

The Neurospora crassa genome encodes two 1,3-α-glucan synthases. One of these 1,3-α-glucan synthase genes, ags-1, was shown to be required for the synthesis of 1,3-α-glucan in the aerial hyphae and macroconidia cell walls. 1,3-α-Glucan was found in the conidia cell wall, but was absent from the vegetative hyphae cell wall. Deletion of ags-1 affected conidial development. Δags-1 produced only 5 % as many conidia as the WT and most of the conidia produced by Δags-1 were not viable. The ags-1 upstream regulatory elements were shown to direct cell-type-specific expression of red fluorescent protein in conidia and aerial hyphae. A haemagglutinin-tagged AGS-1 was found to be expressed in aerial hyphae and conidia. The research showed that 1,3-α-glucan is an aerial hyphae and conidia cell wall component, and is required for normal conidial differentiation.

Tissue-specific expression patterns of nuclear receptors

2013 ◽  
Author(s):  
AL Bookout ◽  
Y Jeong ◽  
M Downes ◽  
RT Yu ◽  
RM Evans ◽  
...  
Keyword(s):  
Nuclear Receptors ◽  
Expression Patterns ◽  
Specific Expression ◽  
Tissue Specific ◽  
Tissue Specific Expression

Probing the 14-3-3 Isoform-Specificity Profile of Interactions Stabilized by Fusicoccin A

2020 ◽  
Author(s):  
James Frederich ◽  
Ananya Sengupta ◽  
Josue Liriano ◽  
Ewa A. Bienkiewicz ◽  
Brian G. Miller
Keyword(s):  
Protein Interactions ◽  
Neurological Diseases ◽  
Adapter Proteins ◽  
Protein Protein Interactions ◽  
Specific Expression ◽  
Individual Client ◽  
Isoform Specificity ◽  
Fusicoccin A

Fusicoccin A (FC) is a fungal phytotoxin that stabilizes protein–protein interactions (PPIs) between 14-3-3 adapter proteins and their phosphoprotein interaction partners. In recent years, FC has emerged as an important chemical probe of human 14-3-3 PPIs implicated in cancer and neurological diseases. These previous studies have established the structural requirements for FC-induced stabilization of 14-3-3·client phosphoprotein complexes; however, the effect of different 14-3-3 isoforms on FC activity has not been systematically explored. This is a relevant question for the continued development of FC variants because there are seven distinct isoforms of 14-3-3 in humans. Despite their remarkable sequence and structural similarities, a growing body of experimental evidence supports both tissue-specific expression of 14-3-3 isoforms and isoform-specific functions <i>in vivo</i>. Herein, we report the isoform-specificity profile of FC <i>in vitro</i>using recombinant human 14-3-3 isoforms and a focused library of fluorescein-labeled hexaphosphopeptides mimicking the C-terminal 14-3-3 recognition domains of client phosphoproteins targeted by FC in cell culture. Our results reveal modest isoform preferences for individual client phospholigands and demonstrate that FC differentially stabilizes PPIs involving 14-3-3s. Together, these data provide strong motivation for the development of non-natural FC variants with enhanced selectivity for individual 14-3-3 isoforms.

Gender-Specific Expression of Arginine-Vasotocin in the Chicken Brain

2004 ◽  
Vol 15 (3) ◽  
pp. 219-223 ◽  
Author(s):  
R. Grossmann ◽  
A. Jurkevich ◽  
S. Klein
Keyword(s):  
Arginine Vasotocin ◽  
Specific Expression ◽  
Chicken Brain ◽  
Gender Specific
Sign in / Sign up

Export Citation Format

Share Document