Screening for cardiac HERG potassium channel interacting proteins using the yeast two‐hybrid technique

2013 ◽  
Vol 38 (2) ◽  
pp. 239-245 ◽  
Author(s):  
Qingyan Ma ◽  
Hong Yu ◽  
Jijin Lin ◽  
Yifan Sun ◽  
Xinyuan Shen ◽  
...  
Keyword(s):  
Potassium Channel ◽  
Hybrid Technique ◽  
Interacting Proteins ◽  
Yeast Two Hybrid ◽  
Two Hybrid

scholarly journals Screening of HBcAg interacting proteins in hepatocytes with yeast-two hybrid technique

2003 ◽  
Vol 11 (4) ◽  
pp. 426-429
Author(s):  
Yin-Ying Lu ◽  
Lin Wang ◽  
Jun Cheng ◽  
Ke Li ◽  
Yan Liu ◽  
...  
Keyword(s):  
Hybrid Technique ◽  
Interacting Proteins ◽  
Yeast Two Hybrid ◽  
Two Hybrid

Identification of PDZ Interactions by Yeast Two-Hybrid Technique

2021 ◽  
pp. 1-15
Author(s):  
Monica Castro-Cruz ◽  
Marta Monserrat-Gomez ◽  
Jean-Paul Borg ◽  
Pascale Zimmermann ◽  
Eric Bailly
Keyword(s):  
Hybrid Technique ◽  
Yeast Two Hybrid ◽  
Two Hybrid

scholarly journals LsHSP70 is induced by high temperature to interact with calmodulin, leading to higher bolting resistance in lettuce

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Ran Liu ◽  
Zhenqi Su ◽  
Huiyan Zhou ◽  
Qian Huang ◽  
Shuangxi Fan ◽  
...  
Keyword(s):  
High Temperature ◽  
High Temperatures ◽  
Morphological Changes ◽  
High Temperature Stress ◽  
Stem Length ◽  
Hybrid Technique ◽  
Yeast Two Hybrid ◽  
Expression Levels ◽  
Two Hybrid ◽  
Lower Expression

Abstract High temperatures have significant impacts on heat-tolerant bolting in lettuce. In this study, it was found that high temperatures could facilitate the accumulation of GA in lettuce to induce bolting, with higher expression levels of two heat shock protein genes LsHsp70-3701 and LsHsp70-2711. By applying VIGS technology, these two Hsp70 genes were incompletely silenced and plant morphological changes under heat treatment of silenced plants were observed. The results showed that lower expression levels of these two genes could enhance bolting stem length of lettuce under high temperatures, which means these two proteins may play a significant role in heat-induced bolting tolerance. By using the yeast two-hybrid technique, it was found that a calmodulin protein could interact with LsHsp70 proteins in a high-temperature stress cDNA library, which was constructed for lettuce. Also, the Hsp70-calmodulin combination can be obtained at high temperatures. According to these results, it can be speculated that the interaction between Hsp70 and calmodulin could be induced under high temperatures and higher GA contents can be obtained at the same time. This study analyses the regulation of heat tolerance in lettuce and lays a foundation for additional studies of heat resistance in lettuce.

Identification of Interacting Proteins Using the Yeast Two-Hybrid Screen

2006 ◽  
pp. 211-232
Author(s):  
Kelly L. Jordan-Sciutto ◽  
Marshall B. Montgomery
Keyword(s):  
Interacting Proteins ◽  
Yeast Two Hybrid ◽  
Two Hybrid

scholarly journals Evaluation of Interactions of Human Cytomegalovirus Immediate-Early IE2 Regulatory Protein with Small Ubiquitin-Like Modifiers and Their Conjugation Enzyme Ubc9

2001 ◽  
Vol 75 (8) ◽  
pp. 3859-3872 ◽  
Author(s):  
Jin-Hyun Ahn ◽  
Yixun Xu ◽  
Won-Jong Jang ◽  
Michael J. Matunis ◽  
Gary S. Hayward
Keyword(s):  
Hcmv Infection ◽  
Dependent Manner ◽  
Interacting Proteins ◽  
Binding Assays ◽  
Yeast Two Hybrid ◽  
Vitro Binding ◽  
Lysine Residues ◽  
Infected Cells ◽  
Two Hybrid

ABSTRACT The human cytomegalovirus (HCMV) major immediate-early protein IE2 is a nuclear phosphoprotein that is believed to be a key regulator in both lytic and latent infections. Using yeast two-hybrid screening, small ubiquitin-like modifiers (SUMO-1, SUMO-2, and SUMO-3) and a SUMO-conjugating enzyme (Ubc9) were isolated as IE2-interacting proteins. In vitro binding assays with glutathioneS-transferase (GST) fusion proteins provided evidence for direct protein-protein interaction. Mapping data showed that the C-terminal end of SUMO-1 is critical for interaction with IE2 in both yeast and in vitro binding assays. IE2 was efficiently modified by SUMO-1 or SUMO-2 in cotransfected cells and in cells infected with a recombinant adenovirus expressing HCMV IE2, although the level of modification was much lower in HCMV-infected cells. Two lysine residues at positions 175 and 180 were mapped as major alternative SUMO-1 conjugation sites in both cotransfected cells and an in vitro sumoylation assay and could be conjugated by SUMO-1 simultaneously. Although mutations of these lysine residues did not interfere with the POD (or ND10) targeting of IE2, overexpression of SUMO-1 enhanced IE2-mediated transactivation in a promoter-dependent manner in reporter assays. Interestingly, many other cellular proteins identified as IE2 interaction partners in yeast two-hybrid assays also interact with SUMO-1, suggesting that either directly bound or covalently conjugated SUMO moieties may act as a bridge for interactions between IE2 and other SUMO-1-modified or SUMO-1-interacting proteins. When we investigated the intracellular localization of SUMO-1 in HCMV-infected cells, the pattern changed from nuclear punctate to predominantly nuclear diffuse in an IE1-dependent manner at very early times after infection, but with some SUMO-1 protein now associated with IE2 punctate domains. However, at late times after infection, SUMO-1 was predominantly detected within viral DNA replication compartments containing IE2. Taken together, these results show that HCMV infection causes the redistribution of SUMO-1 and that IE2 both physically binds to and is covalently modified by SUMO moieties, suggesting possible modulation of both the function of SUMO-1 and protein-protein interactions of IE2 during HCMV infection.

Identification of Connexin-Interacting Proteins: Application of the Yeast Two-Hybrid Screen

Methods ◽  
2000 ◽  
Vol 20 (2) ◽  
pp. 219-231 ◽  
Author(s):  
Chengshi Jin ◽  
Alan F. Lau ◽  
Kendra Dean Martyn
Keyword(s):  
Interacting Proteins ◽  
Yeast Two Hybrid ◽  
Two Hybrid

Yeast Two-Hybrid Assay to Identify Interacting Proteins

2018 ◽  
Vol 95 (1) ◽  
pp. e70 ◽  
Author(s):  
Aurora Paiano ◽  
Azzurra Margiotta ◽  
Maria De Luca ◽  
Cecilia Bucci
Keyword(s):  
Interacting Proteins ◽  
Yeast Two Hybrid ◽  
Two Hybrid
Sign in / Sign up

Export Citation Format

Share Document