| Makale Türü |
|
| 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 |
| Dergi Adı | TURKISH JOURNAL OF BIOLOGY |
| Yayıncı | TUBITAK |
| Açık Erişim | Hayır |
| ISSN | 1300-0152 |
| E-ISSN | 1303-6092 |
| CiteScore | 2,6 |
| SJR | 0,321 |
| SNIP | 0,310 |