Rapid construction of fluorescence quenching-based immunosensor Q-bodies using α-helical coiled-coil peptides

2021 ◽  
Author(s):  
Takanobu Yasuda ◽  
Akihito Inoue ◽  
Tetsuya Kitaguchi ◽  
Hiroshi Ueda
Keyword(s):  
Fluorescence Quenching ◽  
Efficient Method ◽  
Coiled Coil ◽  
Rapid Construction ◽  
Peptide Pair

Here, we report a rapid and efficient method to fabricate Quenchbodies (Q-bodies) that can detect targets with antigen-dependent fluorescence augmentation using a stable coiled-coil peptide pair, E4 and K4 (coiled...

scholarly journals A Non-perturbing Probe of Coiled Coil Formation Based on Electron Transfer Mediated Fluorescence Quenching

Biochemistry ◽  
2016 ◽  
Vol 55 (26) ◽  
pp. 3685-3691 ◽  
Author(s):  
Matthew D. Watson ◽  
Ivan Peran ◽  
Daniel P. Raleigh
Keyword(s):  
Electron Transfer ◽  
Fluorescence Quenching ◽  
Coiled Coil

A heterodimeric coiled-coil peptide pair selected in vivo from a designed library- versus -library ensemble 1 1Edited by A. R. Fersht

2000 ◽  
Vol 295 (3) ◽  
pp. 627-639 ◽  
Author(s):  
Katja M Arndt ◽  
Joelle N Pelletier ◽  
Kristian M Müller ◽  
Tom Alber ◽  
Stephen W Michnick ◽  
...  
Keyword(s):  
Coiled Coil ◽  
Peptide Pair

TMCC3 localizes at the three-way junctions for the proper tubular network of the endoplasmic reticulum

2019 ◽  
Vol 476 (21) ◽  
pp. 3241-3260
Author(s):  
Sindhu Wisesa ◽  
Yasunori Yamamoto ◽  
Toshiaki Sakisaka
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Mammalian Cells ◽  
Coiled Coil ◽  
Transmembrane Domains ◽  
Domain Family ◽  
Coiled Coil Domain ◽  
U2os Cells ◽  
Er Membrane

The tubular network of the endoplasmic reticulum (ER) is formed by connecting ER tubules through three-way junctions. Two classes of the conserved ER membrane proteins, atlastins and lunapark, have been shown to reside at the three-way junctions so far and be involved in the generation and stabilization of the three-way junctions. In this study, we report TMCC3 (transmembrane and coiled-coil domain family 3), a member of the TEX28 family, as another ER membrane protein that resides at the three-way junctions in mammalian cells. When the TEX28 family members were transfected into U2OS cells, TMCC3 specifically localized at the three-way junctions in the peripheral ER. TMCC3 bound to atlastins through the C-terminal transmembrane domains. A TMCC3 mutant lacking the N-terminal coiled-coil domain abolished localization to the three-way junctions, suggesting that TMCC3 localized independently of binding to atlastins. TMCC3 knockdown caused a decrease in the number of three-way junctions and expansion of ER sheets, leading to a reduction of the tubular ER network in U2OS cells. The TMCC3 knockdown phenotype was partially rescued by the overexpression of atlastin-2, suggesting that TMCC3 knockdown would decrease the activity of atlastins. These results indicate that TMCC3 localizes at the three-way junctions for the proper tubular ER network.

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