Using Tripartite Split-sfGFP for the Study of Membrane Protein–Protein Interactions

2020 ◽  
pp. 323-336
Author(s):  
Tzu-Yin Liu
Keyword(s):  
Membrane Protein ◽  
Protein Interactions ◽  
Protein Protein Interactions

Solution Structure of theRhodobacter sphaeroidesPufX Membrane Protein:  Implications for the Quinone Exchange and Protein−Protein Interactions†,‡

Biochemistry ◽  
2007 ◽  
Vol 46 (12) ◽  
pp. 3635-3642 ◽  
Author(s):  
Zheng-Yu Wang ◽  
Hiroaki Suzuki ◽  
Masayuki Kobayashi ◽  
Tsunenori Nozawa
Keyword(s):  
Membrane Protein ◽  
Protein Interactions ◽  
Solution Structure ◽  
Protein Protein Interactions

Detecting Membrane Protein-protein Interactions Using the Mammalian Membrane Two-hybrid (MaMTH) Assay

2017 ◽  
Vol 9 (1) ◽  
pp. 38-54 ◽  
Author(s):  
Punit Saraon ◽  
Ingrid Grozavu ◽  
Sang Hyun Lim ◽  
Jamie Snider ◽  
Zhong Yao ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Two Hybrid

scholarly journals The mechanism of sperm–oocyte fusion in mammals

Reproduction ◽  
2004 ◽  
Vol 127 (4) ◽  
pp. 423-429 ◽  
Author(s):  
Keisuke Kaji ◽  
Akira Kudo
Keyword(s):  
Membrane Protein ◽  
Sexual Reproduction ◽  
Gene Targeting ◽  
Molecular Mechanism ◽  
Protein Interactions ◽  
Recent Progress ◽  
Research Field ◽  
Protein Protein Interactions ◽  
Long Time ◽  
Adams Family

Sperm–oocyte fusion is one of the most impressive events in sexual reproduction, and the elucidation of its molecular mechanism has fascinated researchers for a long time. Because of the limitation of materials and difficulties in analyzing membrane protein–protein interactions, many attempts have failed to reach this goal. Recent studies involving gene targeting have clearly demonstrated the various molecules that are involved in sperm–oocyte binding and fusion. Sperm ADAMs (family of proteins with a disintegrin and metalloprotease domain), including fertilin α, fertilin β and cyritestin, have been investigated and found to be important for binding rather than for fusion and painstaking studies have raised suspicions that their putative receptors, oocyte integrins, are necessary for the sperm–oocyte interaction. Recently, several studies have focused the spotlight on CD9 and glycosylphosphatidylinositol (GPI)-anchored proteins on oocytes, and epididymal protein DE on sperm, as candidate molecules involved in sperm–oocyte fusion. Lack of, or interference with the function of, these proteins can disrupt the sperm–oocyte fusion without changing the binding. In this review we highlight the candidate molecules involved in the sperm–oocyte interaction suggested from the recent progress in this research field.

A proximity-tagging system to identify membrane protein–protein interactions

2018 ◽  
Vol 15 (9) ◽  
pp. 715-722 ◽  
Author(s):  
Qiang Liu ◽  
Jun Zheng ◽  
Weiping Sun ◽  
Yinbo Huo ◽  
Liye Zhang ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Tagging System

scholarly journals Use of G-protein fusions to monitor integral membrane protein–protein interactions in yeast

10.1038/80274 ◽  
2000 ◽  
Vol 18 (10) ◽  
pp. 1075-1079 ◽  
Author(s):  
Kathleen N. Ehrhard ◽  
Jörg J. Jacoby ◽  
Xin-Yuan Fu ◽  
Reinhard Jahn ◽  
Henrik G. Dohlman
Keyword(s):  
Membrane Protein ◽  
G Protein ◽  
Protein Interactions ◽  
Integral Membrane Protein ◽  
Protein Protein Interactions

scholarly journals Novel Topology of BfpE, a Cytoplasmic Membrane Protein Required for Type IV Fimbrial Biogenesis in EnteropathogenicEscherichia coli

2001 ◽  
Vol 183 (15) ◽  
pp. 4435-4450 ◽  
Author(s):  
T. Eric Blank ◽  
Michael S. Donnenberg
Keyword(s):  
Alkaline Phosphatase ◽  
Membrane Protein ◽  
Protein Interactions ◽  
Cytoplasmic Membrane ◽  
Membrane Topology ◽  
Structural Basis ◽  
Protein Protein Interactions ◽  
Type Iv ◽  
C Terminus ◽  
Gradient Fractionation

ABSTRACT Enteropathogenic Escherichia coli (EPEC) produces the bundle-forming pilus (BFP), a type IV fimbria that has been implicated in virulence, autoaggregation, and localized adherence to epithelial cells. The bfpE gene is one of a cluster of bfpgenes previously shown to encode functions that direct BFP biosynthesis. Here, we show that an EPEC strain carrying a nonpolar mutation in bfpE fails to autoaggregate, adhere to HEp-2 cells, or form BFP, thereby demonstrating that BfpE is required for BFP biogenesis. BfpE is a cytoplasmic membrane protein of the GspF family. To determine the membrane topology of BfpE, we fused bfpEderivatives containing 3′ truncations and/or internal deletions to alkaline phosphatase and/or β-galactosidase reporter genes, whose products are active only when localized to the periplasm or cytoplasm, respectively. In addition, we constructed BfpE sandwich fusions using a dual alkaline phosphatase/β-galactosidase reporter cassette and analyzed BfpE deletion derivatives by sucrose density flotation gradient fractionation. The data from these analyses support a topology in which BfpE contains four hydrophobic transmembrane (TM) segments, a large cytoplasmic segment at its N terminus, and a large periplasmic segment near its C terminus. This topology is dramatically different from that of OutF, another member of the GspF family, which has three TM segments and is predominantly cytoplasmic. These findings provide a structural basis for predicting protein-protein interactions required for assembly of the BFP biogenesis machinery.

scholarly journals Characterization of protein–protein interactions between the nucleocapsid protein and membrane protein of the SARS coronavirus

2004 ◽  
Vol 105 (2) ◽  
pp. 121-125 ◽  
Author(s):  
Runtao He ◽  
Andrew Leeson ◽  
Melissa Ballantine ◽  
Anton Andonov ◽  
Lindsay Baker ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Interactions ◽  
Nucleocapsid Protein ◽  
Protein Protein Interactions ◽  
Sars Coronavirus
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