Identification of oxalate oxidase in rice defence system against rice blast

2004 ◽  
Vol 1 (3) ◽  
pp. 167-171 ◽  
Author(s):  
Feng Jie ◽  
Takano Makoto
Keyword(s):  
Disease Resistance ◽  
Protein Kinase ◽  
Rice Blast ◽  
Oxalate Oxidase ◽  
Yeast Two Hybrid ◽  
Gene Encoding ◽  
Yeast Two Hybrid System ◽  
Signal Cascade ◽  
Two Hybrid ◽  
Rice Cdna

AbstractA rice cDNA library was screened using OSK3 protein kinase as bait in a yeast two-hybrid system. The gene encoding oxalate oxidase was one of the positive clones interacting with OSK3 protein kinase. The interactions were verified by detecting expression of the reporter gene lacZ. The results suggest that oxalate oxidase is a downstream element in the disease resistance signal cascade mediated by OSK3 protein kinase in rice.

Protein interactome analysis of 12 mitogen-activated protein kinase kinase kinase in rice using a yeast two-hybrid system

PROTEOMICS ◽  
2014 ◽  
Vol 14 (1) ◽  
pp. 105-115 ◽  
Author(s):  
Raksha Singh ◽  
Jae-Eun Lee ◽  
Sarmina Dangol ◽  
Jihyun Choi ◽  
Ran Hee Yoo ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Hybrid System ◽  
Mitogen Activated Protein Kinase ◽  
Yeast Two Hybrid ◽  
Yeast Two Hybrid System ◽  
Protein Interactome ◽  
Mitogen Activated Protein ◽  
Two Hybrid ◽  
Protein Kinase Kinase

scholarly journals PICK1: a perinuclear binding protein and substrate for protein kinase C isolated by the yeast two-hybrid system.

1995 ◽  
Vol 128 (3) ◽  
pp. 263-271 ◽  
Author(s):  
J Staudinger ◽  
J Zhou ◽  
R Burgess ◽  
S J Elledge ◽  
E N Olson
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Hybrid System ◽  
Catalytic Domain ◽  
Yeast Two Hybrid ◽  
Kinase C ◽  
Yeast Two Hybrid System ◽  
Wide Range ◽  
Two Hybrid

Protein kinase C (PKC) plays a central role in the control of proliferation and differentiation of a wide range of cell types by mediating the signal transduction response to hormones and growth factors. Upon activation by diacylglycerol, PKC translocates to different subcellular sites where it phosphorylates numerous proteins, most of which are unidentified. We used the yeast two-hybrid system to identify proteins that interact with activated PKC alpha. Using the catalytic region of PKC fused to the DNA binding domain of yeast GAL4 as "bait" to screen a mouse T cell cDNA library in which cDNA was fused to the GAL4 activation domain, we cloned several novel proteins that interact with C-kinase (PICKs). One of these proteins, designated PICK1, interacts specifically with the catalytic domain of PKC and is an efficient substrate for phosphorylation by PKC in vitro and in vivo. PICK1 is localized to the perinuclear region and is phosphorylated in response to PKC activation. PICK1 and other PICKs may play important roles in mediating the actions of PKC.

scholarly journals Tomato QM-Like Protein Protects Saccharomyces cerevisiae Cells against Oxidative Stress by Regulating Intracellular Proline Levels

2006 ◽  
Vol 72 (6) ◽  
pp. 4001-4006 ◽  
Author(s):  
Changbin Chen ◽  
Srimevan Wanduragala ◽  
Donald F. Becker ◽  
Martin B. Dickman
Keyword(s):  
Oxidative Stress ◽  
Saccharomyces Cerevisiae ◽  
Ros Generation ◽  
Yeast Two Hybrid ◽  
Gene Encoding ◽  
Yeast Two Hybrid System ◽  
Proapoptotic Protein ◽  
Dehydrogenase Gene ◽  
Two Hybrid ◽  
Overexpressing Strain

ABSTRACT Exogenous proline can protect cells of Saccharomyces cerevisiae from oxidative stress. We altered intracellular proline levels by overexpressing the proline dehydrogenase gene (PUT1) of S. cerevisiae. Put1p performs the first enzymatic step of proline degradation in S. cerevisiae. Overexpression of Put1p results in low proline levels and hypersensitivity to oxidants, such as hydrogen peroxide and paraquat. A put1-disrupted yeast mutant deficient in Put1p activity has increased protection from oxidative stress and increased proline levels. Following a conditional life/death screen in yeast, we identified a tomato (Lycopersicon esculentum) gene encoding a QM-like protein (tQM) and found that stable expression of tQM in the Put1p-overexpressing strain conferred protection against oxidative damage from H2O2, paraquat, and heat. This protection was correlated with reactive oxygen species (ROS) reduction and increased proline accumulation. A yeast two-hybrid system assay was used to show that tQM physically interacts with Put1p in yeast, suggesting that tQM is directly involved in modulating proline levels. tQM also can rescue yeast from the lethality mediated by the mammalian proapoptotic protein Bax, through the inhibition of ROS generation. Our results suggest that tQM is a component of various stress response pathways and may function in proline-mediated stress tolerance in plants.

scholarly journals Rice Mitogen-Activated Protein Kinase Interactome Analysis Using the Yeast Two-Hybrid System

2012 ◽  
Vol 160 (1) ◽  
pp. 477-487 ◽  
Author(s):  
Raksha Singh ◽  
Mi-Ok Lee ◽  
Jae-Eun Lee ◽  
Jihyun Choi ◽  
Ji Hun Park ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Hybrid System ◽  
Mitogen Activated Protein Kinase ◽  
Yeast Two Hybrid ◽  
Yeast Two Hybrid System ◽  
Mitogen Activated Protein ◽  
Two Hybrid

Analysis of interactions between the subunits of protein kinase CK2

1996 ◽  
Vol 74 (4) ◽  
pp. 541-547 ◽  
Author(s):  
David W. Litchfield ◽  
Elzbieta Slominski ◽  
Shawn Lewenza ◽  
Michael Narvey ◽  
Denis G. Bosc ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Hybrid System ◽  
Protein Kinase Ck2 ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Yeast Two Hybrid ◽  
Yeast Two Hybrid System ◽  
Kinase Ck2 ◽  
Α Subunits ◽  
Two Hybrid

Protein kinase CK2, which was formerly known as casein kinase II, is a highly conserved protein serine/threonine kinase implicated in the control of cell proliferation through its phosphorylation of regulatory nuclear proteins. The enzyme consists of catalytic (α and (or) α′) subunits and β subunits that modulate the activity of the catalytic subunits. These subunits are arranged in homotetrameric (i.e., α2β2 or α′2β2) or heterotetrameric (i.e., αα′β2) complexes. We previously demonstrated using the yeast two-hybrid system that α (or α′) subunits can interact with β subunits but not other α (or α′) subunits. By comparison, β subunits can interact with α (or α′) and with β subunits, suggesting that the protein kinase CK2 holoenzyme forms because of the ability of p subunits to dimerize, bringing two heterodimers (αβ or α′β) into a tetrameric complex. In the present study, we used the yeast two-hybrid system to examine the domains of interactions between the α and β subunits of protein kinase CK2. These studies indicate that the ability of β to interact with α resides within the carboxy-terminal domain of β. By comparison, our studies suggest that individual domains of α are not sufficient for interactions with β.Key words: protein kinase CK2, casein kinase II, yeast two-hybrid system, subunit interaction, signal transduction.

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

DETECTION OF MICROCYSTINS BASED ON YEAST TWO-HYBRID SYSTEM

2008 ◽  
Vol 32 (2) ◽  
pp. 201-206
Author(s):  
Xiao PAN
Keyword(s):  
Hybrid System ◽  
Yeast Two Hybrid ◽  
Yeast Two Hybrid System ◽  
Two Hybrid
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