Bacterial toxin colicin N T domain structure changes to ordered state upon binding C terminal domain of TolA      
Yazarlar (5)
Yakup Ulusu
Karamanoğlu Mehmetbey Üniversitesi, Türkiye
Doç. Dr. Sema BİLGİN Tokat Gaziosmanpaşa Üniversitesi, Türkiye
Dr. Öğr. Üyesi Fatma GEDİKLİ Tokat Gaziosmanpaşa Üniversitesi, Türkiye
Jeremy H. Lakey
School Of Medical Education, İngiltere
Isa Gökçe
Tokat Gaziosmanpaşa Üniversitesi, Türkiye
Makale Türü Açık Erişim Özgün Makale
Makale Alt Türü SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale
Dergi Adı Turkish Journal of Biology
Dergi ISSN 1300-0152 Wos Dergi Scopus Dergi
Dergi Tarandığı Indeksler SCI-Expanded
Dergi Grubu Q4
Makale Dili İngilizce
Basım Tarihi 01-2014
Cilt No 38
Sayı 5
Sayfalar 648 / 652
DOI Numarası 10.3906/biy-1401-30
Özet
Colicin N is a bacterial toxin that kills Escherichia coli and related cells. Its mode of action is of interest in protein import and toxicology. Colicin N translocates across the E. coli outer membrane and periplasm by interacting with several receptors. The translocation process involves the interaction of the colicin N with the outer membrane porin OmpF and subsequently with the integral membrane protein TolA. The N-terminal domain of colicin N is involved in the import process. TolA consists of 3 domains. The N-terminal domain of colicin N interacts with the C-terminal domain of TolA at later stages of the translocation process. Our aim was to produce a large quantity of colicin N T-domains for spectroscopic and crystallization studies. These both require a correctly folded and stable protein. Here we present an expression of the complex between the N-terminal domain of colicin N and the C-terminal domain of TolA obtained by fusing these 2 domains with a flexible linker. Circular dichroism spectroscopy studies indicated that unstructured bacterial toxin colicin N T-domains changed to an ordered state upon binding to the C-terminal domain of TolA; this fusion protein has a secondary and tertiary structure.
Anahtar Kelimeler
Colicins | E. coli | Interaction | TolA