Characterization of four C1q/TNF-related proteins (CTRPs) from red-lip mullet (Liza haematocheila) and their transcriptional modulation in response to bacterial and pathogen-associated molecular pattern stimuli

2019 ◽  
Vol 84 ◽  
pp. 158-168 ◽  
Author(s):  
W.K.M. Omeka ◽  
D.S. Liyanage ◽  
Thanthrige Thiunuwan Priyathilaka ◽  
Hyukjae Kwon ◽  
Seongdo Lee ◽  
...  
2021 ◽  
Vol 12 ◽  
Author(s):  
Deepak Duhan ◽  
Shivani Gajbhiye ◽  
Rajdeep Jaswal ◽  
Ravindra Pal Singh ◽  
Tilak Raj Sharma ◽  
...  

Alternaria brassicae is an important necrotrophic pathogen that infects the Brassicaceae family. A. brassicae, like other necrotrophs, also secretes various proteinaceous effectors and metabolites that cause cell death to establish itself in the host. However, there has been no systematic study of A. brassicae effectors and their roles in pathogenesis. The availability of the genome sequence of A. brassicae in public domain has enabled the search for effectors and their functional characterization. Nep1-like proteins (NLPs) are a superfamily of proteins that induce necrosis and ethylene biosynthesis. They have been reported from a variety of microbes including bacteria, fungi, and oomycetes. In this study, we identified two NLPs from A. brassicae viz. AbrNLP1 and AbrNLP2 and functionally characterized them. Although both AbrNLPs were found to be secretory in nature, they localized differentially inside the plant. AbrNLP2 was found to induce necrosis in both host and non-host species, while AbrNLP1 could not induce necrosis in both species. Additionally, AbrNLP2 was shown to induce pathogen-associated molecular pattern (PAMP)-triggered immunity in both host and non-host species. Overall, our study indicates that AbrNLPs are functionally and spatially (subcellular location) distinct and may play different but important roles during the pathogenesis of A. brassicae.


1996 ◽  
Vol 96 (4) ◽  
pp. 585-592 ◽  
Author(s):  
Randal W. Giroux ◽  
K. Peter Pauls

2018 ◽  
Vol 20 (1) ◽  
pp. 93
Author(s):  
Jin Wang ◽  
Feiyi Huang ◽  
Xiong You ◽  
Xilin Hou

In plants, heptahelical proteins (HHPs) have been shown to respond to a variety of abiotic stresses, including cold stress. Up to the present, the regulation mechanism of HHP5 under low temperature stress remains unclear. In this study, BcHHP5 was isolated from Pak-choi (Brassica rapa ssp. chinensis cv. Suzhouqing). Sequence analysis and phylogenetic analysis indicated that BcHHP5 in Pak-choi is similar to AtHHP5 in Arabidopsis thaliana. Structure analysis showed that the structure of the BcHHP5 protein is relatively stable and highly conservative. Subcellular localization indicated that BcHHP5 was localized on the cell membrane and nuclear membrane. Furthermore, real-time quantitative polymerase chain reaction (RT-qPCR) analysis showed that BcHHP5 was induced to express by cold and other abiotic stresses. In Pak-choi, BcHHP5-silenced assay, inhibiting the action of endogenous BcHHP5, indicated that BcHHP5-silenced might have a negative effect on cold tolerance, which was further confirmed. All of these results indicate that BcHHP5 might play a role in abiotic response. This work can serve as a reference for the functional analysis of other cold-related proteins from Pak-choi in the future.


1991 ◽  
Vol 11 (10) ◽  
pp. 5113-5124 ◽  
Author(s):  
H Wu ◽  
A B Reynolds ◽  
S B Kanner ◽  
R R Vines ◽  
J T Parsons

Transformation of cells by the src oncogene results in elevated tyrosine phosphorylation of two related proteins, p80 and p85 (p80/85). Immunostaining with specific monoclonal antibodies revealed a striking change of subcellular localization of p80/85 in src-transformed cells. p80/85 colocalizes with F-actin in peripheral extensions of normal cells and rosettes (podosomes) of src-transformed cells. Sequence analysis of cDNA clones encoding p80/85 revealed an amino-terminal domain composed of six copies of a direct tandem repeat, each repeat containing 37 amino acids, a carboxyl-terminal SH3 domain, and an interdomain region composed of a highly charged acidic region and a region rich in proline, serine, and threonine. The multidomain structure of p80/85 and its colocalization with F-actin in normal and src-transformed cells suggest that these proteins may associate with components of the cytoskeleton and contribute to organization of cell structure.


2013 ◽  
Vol 64 (12) ◽  
pp. 3615-3625 ◽  
Author(s):  
Mathieu Larroque ◽  
Elodie Belmas ◽  
Thomas Martinez ◽  
Sophie Vergnes ◽  
Nathalie Ladouce ◽  
...  

2012 ◽  
Vol 355 (1) ◽  
pp. 143-152 ◽  
Author(s):  
Sirawut Klinbunga ◽  
Sasithorn Petkorn ◽  
Suthathip Kittisenachai ◽  
Narumon Phaonakrop ◽  
Sittiruk Roytrakul ◽  
...  

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