Difference between revisions of "Part:BBa I732103"
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[[Image:USTC_1l1m_bio_r_500.jpg|thumb|150px|'''Figure 1''' Solution structure of a dimer of Lac repressor DNA-binding domain complexed to its natural operator O1 ([http://www.rcsb.org/pdb/explore.do?structureId=1L1M From RCSB])]] | [[Image:USTC_1l1m_bio_r_500.jpg|thumb|150px|'''Figure 1''' Solution structure of a dimer of Lac repressor DNA-binding domain complexed to its natural operator O1 ([http://www.rcsb.org/pdb/explore.do?structureId=1L1M From RCSB])]] | ||
− | The | + | [[Image:USTC_MullerRepression.png|thumb|center|300px|'''Figure I''' Repression Metrix(RM):The repression matrix reveals the binding affinity of different repressor candidates with various specific promoters by different colors. The deeper the red will be, the higher the repression will appear. While the lighter the blue is the weaker the repression will show. This Matrix are not directly from literatures but from the data by previous research work.]] |
− | + | The sequence produce LRLb repressor protein which is based on natural lacR with only several point mutations. Standard BioBrick Prefix and Suffix are added to both ends of this part for standard assembly. | |
− | + | ||
+ | ===Usage and Biology=== | ||
+ | Refer to the Repression Matrix on the above, we picked up 4 well-performing repressors as candidates to do our study; they are LRLa, LRLb, LRLc, LRLd. | ||
(''Reference'': | (''Reference'': | ||
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2.Lehming, N.; Sartorius, J.; Oehler, S.; von Wilcken-Bergmann, B. & Müller-Hill, B. Recognition helices of lac and lambda repressor are oriented in opposite directions and recognize similar DNA sequences. PNAS, 1988, 85, 7947-7951 | 2.Lehming, N.; Sartorius, J.; Oehler, S.; von Wilcken-Bergmann, B. & Müller-Hill, B. Recognition helices of lac and lambda repressor are oriented in opposite directions and recognize similar DNA sequences. PNAS, 1988, 85, 7947-7951 | ||
3. Sartorius, J.; Lehming, N.; Kisters, B.; von Wilcken-Bergmann, B. & Müller-Hill, B. (1989), 'lac repressor mutants with double or triple exchanges in the recognition helix bind specifically to lac operator variants with multiple exchanges.', EMBO J 8(4), 1265--1270.) | 3. Sartorius, J.; Lehming, N.; Kisters, B.; von Wilcken-Bergmann, B. & Müller-Hill, B. (1989), 'lac repressor mutants with double or triple exchanges in the recognition helix bind specifically to lac operator variants with multiple exchanges.', EMBO J 8(4), 1265--1270.) | ||
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Revision as of 07:00, 26 October 2007
LacI
The sequence produce LRLb repressor protein which is based on natural lacR with only several point mutations. Standard BioBrick Prefix and Suffix are added to both ends of this part for standard assembly.
Usage and Biology
Refer to the Repression Matrix on the above, we picked up 4 well-performing repressors as candidates to do our study; they are LRLa, LRLb, LRLc, LRLd.
(Reference: 1.Lewis, M. (2005), 'The lac repressor.', C R Biol 328 (6), 521--548. 2.Lehming, N.; Sartorius, J.; Oehler, S.; von Wilcken-Bergmann, B. & Müller-Hill, B. Recognition helices of lac and lambda repressor are oriented in opposite directions and recognize similar DNA sequences. PNAS, 1988, 85, 7947-7951 3. Sartorius, J.; Lehming, N.; Kisters, B.; von Wilcken-Bergmann, B. & Müller-Hill, B. (1989), 'lac repressor mutants with double or triple exchanges in the recognition helix bind specifically to lac operator variants with multiple exchanges.', EMBO J 8(4), 1265--1270.)
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]