scholarly journals Identification of a Plum pox virus CI-Interacting Protein from Chloroplast That Has a Negative Effect in Virus Infection

2006 ◽  
Vol 19 (3) ◽  
pp. 350-358 ◽  
Author(s):  
I. Jiménez ◽  
L. López ◽  
J. M. Alamillo ◽  
A. Valli ◽  
J. A. García
Keyword(s):  
Nicotiana Benthamiana ◽  
Cell Movement ◽  
Host Factors ◽  
Plum Pox Virus ◽  
Yeast Two Hybrid ◽  
Interacting Protein ◽  
Yeast Two Hybrid System ◽  
Negative Effect ◽  
Virus Interactions ◽  
Two Hybrid

The cylindrical inclusion (CI) protein of potyviruses is involved in virus replication and cell-to-cell movement. These two processes should rely on multiple plant-virus interactions; however, little is known about the host factors that are involved in, or that may interfere with, CI functions. By using a yeast two-hybrid system, the CI protein from Plum pox virus (PPV) was found to interact with the photosystem I PSI-K protein, the product of the gene psaK, of Nicotiana benthamiana. Coexpression of PPV CI was shown to cause a decrease in the accumulation level of PSI-K transiently expressed in N. benthamiana leaves. To test the biological relevance of this interaction, we have analyzed the infection of PPV in N. benthamiana plants in which psaK gene expression has been silenced by RNA interference, as well as in Arabidopsis thaliana psaK knockout plants. Our results show that downregulation of the psaK gene leads to higher PPV accumulation, suggesting a role for the CI-PSI-K interaction in PPV infection.

Fishing TaSC Interacting Protein in Wheat Using Split Ubiquitin Yeast Two Hybrid System

2013 ◽  
Vol 39 (3) ◽  
pp. 423
Author(s):  
Fang-Fang LIN ◽  
Xu YANG ◽  
Xiao-Cui WU ◽  
Xiao-Mei LIU ◽  
Rong-Chao GE ◽  
...  
Keyword(s):  
Hybrid System ◽  
Yeast Two Hybrid ◽  
Interacting Protein ◽  
Yeast Two Hybrid System ◽  
Split Ubiquitin ◽  
Two Hybrid

scholarly journals 14-3-3ζ interacts with the α-chain of human interleukin 9 receptor

2000 ◽  
Vol 345 (3) ◽  
pp. 741-747 ◽  
Author(s):  
Daniel SLIVA ◽  
Minyi GU ◽  
Yuan Xiao ZHU ◽  
Jun CHEN ◽  
Schickwann TSAI ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Hybrid System ◽  
Potential Role ◽  
Tyrosine Kinase Receptor ◽  
Yeast Two Hybrid ◽  
Interacting Protein ◽  
Yeast Two Hybrid System ◽  
Α Chain ◽  
Interleukin 9 ◽  
Two Hybrid

Interleukin 9 (IL-9) exerts its pleiotropic effects through the IL-9 receptor (IL-9R) complex, which consists of the IL-9R α-chain, which determines the cytokine specificity, and the IL-2 receptor γ-chain. In the present study we used a modified yeast two-hybrid system to isolate cDNA species encoding proteins that interacted with the intracellular domain of the human IL-9R α-chain (hIL-9Rα). We have identified 14-3-3ζ as an hIL-9Rα-interacting protein. We also mapped residues 518-522 (Arg-Ser519-Trp-Thr521-Phe) in hIL-9Rα and helix I of 14-3-3ζ as being important for interaction. Moreover, peptide competition experi-ments suggested that interaction between hIL-9Rα and 14-3-3ζ requires the phosphorylation of Ser519 or Thr521. This is the first demonstration that 14-3-3 can interact with a non-tyrosine kinase receptor. The interaction between 14-3-3 and IL-9Rα but not IL-4Rα also suggests a potential role for 14-3-3 in determining cytokine specificity.

scholarly journals Interaction of CSFV E2 Protein with Swine Host Factors as Detected by Yeast Two-Hybrid System

PLoS ONE ◽  
2014 ◽  
Vol 9 (1) ◽  
pp. e85324 ◽  
Author(s):  
Douglas P. Gladue ◽  
Ryan Baker-Bransetter ◽  
Lauren G. Holinka ◽  
Ignacio J. Fernandez-Sainz ◽  
Vivian O’Donnell ◽  
...  
Keyword(s):  
Hybrid System ◽  
Host Factors ◽  
Yeast Two Hybrid ◽  
E2 Protein ◽  
Yeast Two Hybrid System ◽  
Two Hybrid

scholarly journals The Membrane-Associated Guanylate Kinase Protein MAGI-1 Binds Megalin and Is Present in Glomerular Podocytes

2001 ◽  
Vol 12 (4) ◽  
pp. 667-677 ◽  
Author(s):  
KEVIN M. PATRIE ◽  
ANDREW J. DRESCHER ◽  
MEERA GOYAL ◽  
ROGER C. WIGGINS ◽  
BEN MARGOLIS
Keyword(s):  
Pdz Domain ◽  
Specific Protein ◽  
Yeast Two Hybrid ◽  
Guanylate Kinase ◽  
Interacting Protein ◽  
Yeast Two Hybrid System ◽  
Adult Kidney ◽  
Two Hybrid ◽  
Close Homolog ◽  
Dependent Interaction

Abstract. The transmembrane endocytic receptor glycoprotein 330/megalin (hereafter referred to as megalin) is localized to the apical membrane domain of epithelial cells, where it is involved in the uptake of proteins from extracellular sources. The cytoplasmic domain of megalin contains amino acid motifs that have the potential to bind to other proteins, which may influence its localization or function. The yeast two-hybrid system was used to search for proteins that bind to the cytoplasmic tail of megalin, and a protein fragment from a mouse embryonic cDNA library that contained a single PDZ domain was identified. This protein, which was namedglycoprotein 330-associatedprotein (GASP), appears to be a truncated mouse counterpart of the human and rat proteins atrophin-1-interacting protein-1 and synaptic scaffolding molecule, respectively. The interaction of GASP with megalin is mediated by the PDZ domain of GASP binding to the DSDV motif found at the carboxyl-terminus of megalin. A mutant version of megalin that lacks the terminal valine is unable to bind to GASP, illustrating the PDZ domain-dependent interaction between these two proteins. A close homolog of GASP,i.e., membrane-associated guanylate kinase with inverted orientation-1 (MAGI-1), is more ubiquitous in its tissue distribution (including kidney) and is also able to specifically bind to megalin via its fifth PDZ domain. Immunofluorescence studies of adult kidney revealed that MAGI-1 is expressed in the glomerulus of the kidney, in a manner that parallels the expression of the podocyte-specific protein glomerular epithelial protein 1. Western analysis of endogenous MAGI-1 from glomerular preparations suggests that it is associated with the cytoskeleton and seems to be expressed in a different form, compared with cell line-derived endogenous MAGI-1. The association of megalin with MAGI-1 may allow the assembly of a multiprotein complex, in which megalin may serve a nonendocytic function in glomerular podocytes.

scholarly journals HIP-I: A huntingtin interacting protein isolated by the yeast two-hybrid system

1997 ◽  
Vol 6 (3) ◽  
pp. 487-495 ◽  
Author(s):  
E. E. Wanker ◽  
C. Rovira ◽  
E. Scherzinger ◽  
R. Hasenbank ◽  
S. Walter ◽  
...  
Keyword(s):  
Hybrid System ◽  
Yeast Two Hybrid ◽  
Interacting Protein ◽  
Yeast Two Hybrid System ◽  
Huntingtin Interacting Protein ◽  
Two Hybrid

Identifications of DNA Sequences Encoding Key Region of SCR Interacting with SRK Extracellular Domain by Using Yeast Two-Hybrid System

2013 ◽  
Vol 38 (9) ◽  
pp. 1583-1591
Author(s):  
Li-Yan XUE ◽  
Bing LUO ◽  
Li-Quan ZHU ◽  
Yong-Jun YANG ◽  
He-Cui ZHANG ◽  
...  
Keyword(s):  
Hybrid System ◽  
Dna Sequences ◽  
Extracellular Domain ◽  
Yeast Two Hybrid ◽  
Yeast Two Hybrid System ◽  
Two Hybrid

scholarly journals Implication of the Whitefly Protein Vps Twenty Associated 1 (Vta1) in the Transmission of Cotton Leaf Curl Multan Virus

2021 ◽  
Vol 9 (2) ◽  
pp. 304
Author(s):  
Yao Chi ◽  
Li-Long Pan ◽  
Shu-Sheng Liu ◽  
Shahid Mansoor ◽  
Xiao-Wei Wang
Keyword(s):  
Coat Protein ◽  
Molecular Mechanisms ◽  
Cotton Leaf ◽  
Yeast Two Hybrid ◽  
Yeast Two Hybrid System ◽  
Vacuolar Protein ◽  
Leaf Curl Disease ◽  
Two Hybrid ◽  
Asia Ii 1 ◽  
Leaf Curl

Cotton leaf curl Multan virus (CLCuMuV) is one of the major casual agents of cotton leaf curl disease. Previous studies show that two indigenous whitefly species of the Bemisia tabaci complex, Asia II 1 and Asia II 7, are able to transmit CLCuMuV, but the molecular mechanisms underlying the transmission are poorly known. In this study, we attempted to identify the whitefly proteins involved in CLCuMuV transmission. First, using a yeast two-hybrid system, we identified 54 candidate proteins of Asia II 1 that putatively can interact with the coat protein of CLCuMuV. Second, we examined interactions between the CLCuMuV coat protein and several whitefly proteins, including vacuolar protein sorting-associated protein (Vps) twenty associated 1 (Vta1). Third, using RNA interference, we found that Vta1 positively regulated CLCuMuV acquisition and transmission by the Asia II 1 whitefly. In addition, we showed that the interaction between the CLCuMuV coat protein and Vta1 from the whitefly Middle East-Asia Minor (MEAM1), a poor vector of CLCuMuV, was much weaker than that between Asia II 1 Vta1 and the CLCuMuV coat protein. Silencing of Vta1 in MEAM1 did not affect the quantity of CLCuMuV acquired by the whitefly. Taken together, our results suggest that Vta1 may play an important role in the transmission of CLCuMuV by the whitefly.

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