Difference between revisions of "Part:BBa K346004:Design"
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===Design Notes=== | ===Design Notes=== | ||
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| + | [[Image:construction of MBP(lead).jpg]] | ||
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| + | Similar method as MBP(mercury) is constructed was applied to PbrR. Firstly,Sequence alignment of MerR and PbrR has been carried out. Previous work showed that MerR family TFs share a highly conserved homology at their metal binding domains (Brown et al., 2003; Hobman, 2007), which implies that our strategies of bioabsorbent engineering might be applicable to other cases of heavy metals. We again design a single polypeptide consisting of two dimerization helixes and metal binding loops of PbrR, to form an antiparallel coiled coil MBP mimicking the dimerized metal binding domains of the wild-type as Figure(B) shows.Figure (C) shows that the MBP was constructed by fusing two copies of metal binding domain of PbrR in tandem via the same method with mercury MBP. | ||
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===Source=== | ===Source=== | ||
| − | + | Pro. Chuan He | |
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===References=== | ===References=== | ||
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| + | Brown, N. L., Stoyanov, J. V. & Kidd, S. P. & Hobman, J. L. The MerR family of transcriptional regulators. FEMS Microbiol. Rev. 27, 145-163 (2003). | ||
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| + | Zeng, Q., Stalhandske, C., Anderson, M. C., Scott, R. A. & Summers, A. O. The core metal-recognition domain of MerR. Biochemistry 37, 15885-15895 (1998). | ||
| + | |||
| + | Mejare, M. & Bulow, L. Metal-binding proteins and peptides in bioremediation and phytoremediation of heavy metals. Trends in biotechnol. 19, 67-73(2001). | ||
Revision as of 04:39, 25 October 2010
RBS(B0034)_MBP(lead metal binding peptide egineered from PbrR)+Terminator(B0015)
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Design Notes
.jpg)
Similar method as MBP(mercury) is constructed was applied to PbrR. Firstly,Sequence alignment of MerR and PbrR has been carried out. Previous work showed that MerR family TFs share a highly conserved homology at their metal binding domains (Brown et al., 2003; Hobman, 2007), which implies that our strategies of bioabsorbent engineering might be applicable to other cases of heavy metals. We again design a single polypeptide consisting of two dimerization helixes and metal binding loops of PbrR, to form an antiparallel coiled coil MBP mimicking the dimerized metal binding domains of the wild-type as Figure(B) shows.Figure (C) shows that the MBP was constructed by fusing two copies of metal binding domain of PbrR in tandem via the same method with mercury MBP.
Source
Pro. Chuan He
References
Brown, N. L., Stoyanov, J. V. & Kidd, S. P. & Hobman, J. L. The MerR family of transcriptional regulators. FEMS Microbiol. Rev. 27, 145-163 (2003).
Zeng, Q., Stalhandske, C., Anderson, M. C., Scott, R. A. & Summers, A. O. The core metal-recognition domain of MerR. Biochemistry 37, 15885-15895 (1998).
Mejare, M. & Bulow, L. Metal-binding proteins and peptides in bioremediation and phytoremediation of heavy metals. Trends in biotechnol. 19, 67-73(2001).