Bimolecular fluorescence complementation assay to explore protein- protein interactions of the Yersinia virulence factor YopM
Küçük Resim Yok
Tarih
2021
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Academic Press Inc Elsevier Science
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
Yersinia outer protein M (YopM) is one of the effector proteins and essential for virulence. YopM is delivered by the Yersinia type III secretion system (T3SS) into the host cell, where it shows immunosuppressive effect through interaction with host proteins. Therefore, protein-protein interactions of YopM is significant to understand its molecular mechanism. In this study, we aimed to explore protein protein interactions of YopM with the two components of T3SS, namely LcrV and LcrG. We used bimolecular fluorescence complementation (BiFC) assay and monitored the reassembly of green fluorescence protein in Escherichia coli. As an indicator of the protein-protein interaction, we monitored the in vivo reconstitution of fluorescence by measuring fluorescence intensity and imaging the cells under fluorescence microscope. We showed, for the first time, that YopM interacts with LcrG, but not with LcrV. Here, we propose BiFC assay as a simple method to screen novel interaction partners of YopM. (c) 2021 Elsevier Inc. All rights reserved.
Açıklama
Anahtar Kelimeler
Protein interaction, Fluorescence, Green fluorescent protein, Protein complementation, Effector protein, Iii Secretion System, Host Kinases, Pestis, Bifc, Lcrv, Enterocolitica, Visualization, Model, Tool
Kaynak
Biochemical and Biophysical Research Communications
WoS Q Değeri
Q3
Scopus Q Değeri
Q1
Cilt
582
