Display of membrane proteins on the heterologous caveolae carved by caveolin-1 in the Escherichia coli cytoplasm

作者：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^*

来源：Enzyme and Microbial Technology, 2015, 79-80: 55-62.

DOI：10.1016/j.enzmictec.2015.06.018

• Caveolin-1
• Heterologous caveolae
• Transmembrane protein

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.

• 出版日期2015-11