Difference between revisions of "Part:BBa K3093004"
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The α-hemolysin secretion pathway has mainly been reported in uropathogenic E. coli. The secretory machinery of this pathway consists of three components: HlyB, an ATP-binding cassette (ABC transporter); HlyD, a membrane fusion protein; and TolC, an outer membrane protein. HlyB and HlyD have been generally considered strain specific proteins, TolC, in contrast, is a component of multiple trans-membrane systems in many microorganisms. Thus, co-expression of HlyB/D is often performed to facilitate the extracellular translocation of proteins utilizing the α-hemolysin secretion pathway during expression in host strains other than uropathogenic E. coli. | The α-hemolysin secretion pathway has mainly been reported in uropathogenic E. coli. The secretory machinery of this pathway consists of three components: HlyB, an ATP-binding cassette (ABC transporter); HlyD, a membrane fusion protein; and TolC, an outer membrane protein. HlyB and HlyD have been generally considered strain specific proteins, TolC, in contrast, is a component of multiple trans-membrane systems in many microorganisms. Thus, co-expression of HlyB/D is often performed to facilitate the extracellular translocation of proteins utilizing the α-hemolysin secretion pathway during expression in host strains other than uropathogenic E. coli. | ||
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===Usage and Biology=== | ===Usage and Biology=== | ||
Revision as of 14:46, 19 October 2019
HlyD
The α-hemolysin secretion pathway has mainly been reported in uropathogenic E. coli. The secretory machinery of this pathway consists of three components: HlyB, an ATP-binding cassette (ABC transporter); HlyD, a membrane fusion protein; and TolC, an outer membrane protein. HlyB and HlyD have been generally considered strain specific proteins, TolC, in contrast, is a component of multiple trans-membrane systems in many microorganisms. Thus, co-expression of HlyB/D is often performed to facilitate the extracellular translocation of proteins utilizing the α-hemolysin secretion pathway during expression in host strains other than uropathogenic E. coli.
Usage and Biology
In order to utilize the less useful shortened cellulose from wastepaper as the raw material to produce bacterial cellulose(BC) in situ, ECUST iGEMers developed “paper transformer”. It was a dual plasmid system(pCL-pCS) including four parts : 1. Cellulose hydrolysis, 2. BC synthesis, 3. Inverter system, 4. Cellobiose response element. We chose E.coli DH5α as the chassis.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]