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Display of membrane proteins on the heterologous caveolae carved by caveolin-1 in the Escherichia coli cytoplasm
- Display of membrane proteins on the heterologous caveolae carved by caveolin-1 in the Escherichia coli cytoplasm
- Shin, Jonghyeok; Jung, Young-Hun; Cho, Da-Hyeong; Park, Myungseo; Lee, Kyung Eun; Yang, Yoosoo; Jeong, Cherlhyun; Sung, Bong Hyun; Sohn, Jung-Hoon; Park, Jin-Byung; Kweon, Dae-Hyuk
- Ewha Authors
- SCOPUS Author ID
- Issue Date
- Journal Title
- ENZYME AND MICROBIAL TECHNOLOGY
- 0141-0229; 1879-0909
- vol. 79-80, pp. 55 - 62
- Caveolin-1; Heterologous caveolae; Transmembrane protein
- ELSEVIER SCIENCE INC
- SCI; SCIE; SCOPUS
- Caveolae are membrane-budding structures that exist in many vertebrate cells. One of the important functions of caveolae is to form membrane curvature and endocytic vesicles. Recently, it was shown that caveolae-like structures were formed in Escherichia coli through the expression of caveolin-1. This interesting structure seems to be versatile for a variety of biotechnological applications. Targeting of heterologous proteins in the caveolae-like structure should be the first question to be addressed for this purpose. Here we show that membrane proteins co-expressed with caveolin-1 are embedded into the heterologous caveolae (h-caveolae), the cavaolae-like structures formed inside the cell. Two transmembrane SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, Syntaxin la and vesicle-associated membrane protein 2 (VAMP2), were displayed on the h-caveolae surface. The size of the h-caveolae harboring the transmembrane proteins was similar to 100 nm in diameter. The proteins were functional and faced outward on the h-caveolae. Multi-spanning transmembrane proteins FtsH and FeoB could be included in the h-caveolae, too. Furthermore, the recombinant E. coli cells were shown to endocytose substrate supplemented in the medium. These results provide a basis for exploiting the h-caveolae formed inside E. coli cells for future biotechnological applications. (C) 2015 Elsevier Inc. All rights reserved.
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