Difference between revisions of "Part:BBa K2912000"

Revision as of 16:28, 23 September 2019

RebA may act as a scaffolding protein to facilitate the major polymerization process

SZU-China 2019 iGEM team was going to find a suicide switch inside the E coli that can break the whole body of the bacteria leading to the release of RNAi molecules transcribed from E coli inducing by IPTG or some other else. Therefore, we were in need the useful mechanism. Fortunately, we finally found the Refractile inclusion bodies (R-bodies) to kill the E coli, causing the inclusion to flow out of the plasma membrane, so that we can get the RNAi molecules transcribed by E coli.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

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 <partinfo>BBa_K2912000 short</partinfo>
-Refractile inclusion bodies, known as R bodies, are produced by only a few species of bacteria. These inclusion bodies are highly insoluble protein ribbons, typically seen coiled into cylindrical structures within the cell. R-bodies are produced by Paramecium endosymbionts belonging to the genus Caedibacter. These intracellular bacteria confer upon their hosts a phenomenon called the killer trait. This is one of the DNA sequences for the R body locus (reb) from Caedibacter taeniospiralis. It has been suggested that RebA may act as a scaffolding protein to facilitate the major polymerization process.The identity in amino acid sequence between RebA and RebB suggests a similar structure and function. Like RebB, RebA is modified into two or more species with different molecular weights before the major polymerization event occurs.
+SZU-China 2019 iGEM team was going to find a suicide switch inside the E coli that can break the whole body of the bacteria leading to the release of RNAi molecules transcribed from E coli inducing by IPTG or some other else. Therefore, we were in need the useful mechanism. Fortunately, we finally found the Refractile inclusion bodies (R-bodies) to kill the E coli, causing the inclusion to flow out of the plasma membrane, so that we can get the RNAi molecules transcribed by E coli.
-Comparison of the hydropathy plots for RebB with those for RebA suggests a similar secondary structure for these regions. Therefore, RebA should be capable of entering into either a temporary or permanent association with the polymerized complexes of RebB. If the acidic RebA proteins are linked to the growing R body complex (as scaffolding or at the site of polymerization), they may be responsible for the increased pIs during the major polymerization event. That is, the proportional contribution of RebA may decline as polymerization proceeds, resulting in a shift of the pls. Pulse-chase analysis of the protein products encoded by pBQ65 reveals that, like RebB, the modified faster-migrating species of RebA decrease in concentration over time as the higher-molecular-weight polymerization complexes are formed. This is evidence that RebA proteins may associate directly with the polymerization complexes.
 <!-- Add more about the biology of this part here
 ===Usage and Biology===
+Refractile inclusion bodies, known as R bodies, are produced by only a few species of bacteria. These inclusion bodies are highly insoluble protein ribbons, typically seen coiled into cylindrical structures within the cell[1]. R-bodies are produced by Paramecium endosymbionts belonging to the genus Caedibacter. These intracellular bacteria confer upon their hosts a phenomenon called the killer trait[2]. This is one of the DNA sequences for the R body locus (reb) from Caedibacter taeniospiralis. It has been suggested that Reb A may act as a scaffolding protein to facilitate the major polymerization process. The identity in amino acid sequence between Reb A and Reb B suggests a similar structure and function. Like Reb B, Reb A is modified into two or more species with different molecular weights before the major polymerization event occurs[3].
+Comparison of the hydropathy plots for Reb B with those for Reb A suggests a similar secondary structure for these regions. Therefore, Reb A should be capable of entering either a temporary or permanent association with the polymerized complexes of Reb B. If the acidic Reb A proteins are linked to the growing R body complex (as scaffolding or at the site of polymerization), they may be responsible for the increased pIs during the major polymerization event. That is, the proportional contribution of Reb A may decline as polymerization proceeds, resulting in a shift of the pls. Pulse-chase analysis of the protein products encoded by pBQ65 reveals that, like Reb B, the modified faster-migrating species of Reb A decrease in concentration over time as the higher-molecular-weight polymerization complexes are formed. This is evidence that Reb A proteins may associate directly with the polymerization complexes[3].
+The R bodies of C. taeniospiralis are type 51. They are about 0.5 μm wide, have a maximum length of 20 μm, and 13 nm thick, possess acute angles at each end, and unroll in a telescopic fashion when exposed to a pH of 6.5 or lower. These proteinaceous ribbons are rolling up inside the cell to form a hollow cylinder about 0.5 μm in diameter and 0.5 μm long[4]. For more information, please see BBa_K2912003.
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