Difference between revisions of "Part:BBa K4140015"
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A common structural motif identified in functioning RNA species is the kink-turn (k-turn). It typically consists of a tandem trans sugar edge-Hoogsteen G followed by a three-nucleotide bulge: pair A bases. The minor grooves are juxtaposed and the axis of duplex RNA is given a strong bend. The conserved adenine nucleobases of the G:A basepairs accept the cross-strand H-bonds that form at the interface. The k-turns are split into two conformational classes, N3 and N1, by alternative acceptors for one of these. The conformation that a specific k-turn adopts is determined by the base pair (3b:3n) that follows the G:A pairings. K-turns typically bind proteins and mediate tertiary contacts in folded RNA species. Members of the L7Ae family of proteins are frequently found to bind k-turns | A common structural motif identified in functioning RNA species is the kink-turn (k-turn). It typically consists of a tandem trans sugar edge-Hoogsteen G followed by a three-nucleotide bulge: pair A bases. The minor grooves are juxtaposed and the axis of duplex RNA is given a strong bend. The conserved adenine nucleobases of the G:A basepairs accept the cross-strand H-bonds that form at the interface. The k-turns are split into two conformational classes, N3 and N1, by alternative acceptors for one of these. The conformation that a specific k-turn adopts is determined by the base pair (3b:3n) that follows the G:A pairings. K-turns typically bind proteins and mediate tertiary contacts in folded RNA species. Members of the L7Ae family of proteins are frequently found to bind k-turns | ||
==Usage== | ==Usage== | ||
| − | using K-turns' capacity to mediate tertiary contacts in folded RNA species and bind proteins. As a result, we employ it to regulate the expression of our CRISPR regulatory system since, when combined with L7Ae, it suppresses the translation of the protein portion (Cas12g), Whenever there is a high quantity of phenylalanine. | + | using K-turns' capacity to mediate tertiary contacts in folded RNA species and bind proteins. As a result, we employ it to regulate the expression of our CRISPR regulatory system since, when combined with L7Ae, it suppresses the translation of the protein portion (Cas12g), Whenever there is a high quantity of phenylalanine as shown in figure 1. |
| + | |||
| + | [[Image:reg.png|thumb|right|Figure(1) Shows an SBOL demonstrating the usage of k-turns in our whole cel-based biosensor ]] | ||
==Literature Characterization== | ==Literature Characterization== | ||
Revision as of 13:08, 7 October 2022
Kink turn
Part Description
A common structural motif identified in functioning RNA species is the kink-turn (k-turn). It typically consists of a tandem trans sugar edge-Hoogsteen G followed by a three-nucleotide bulge: pair A bases. The minor grooves are juxtaposed and the axis of duplex RNA is given a strong bend. The conserved adenine nucleobases of the G:A basepairs accept the cross-strand H-bonds that form at the interface. The k-turns are split into two conformational classes, N3 and N1, by alternative acceptors for one of these. The conformation that a specific k-turn adopts is determined by the base pair (3b:3n) that follows the G:A pairings. K-turns typically bind proteins and mediate tertiary contacts in folded RNA species. Members of the L7Ae family of proteins are frequently found to bind k-turns
Usage
using K-turns' capacity to mediate tertiary contacts in folded RNA species and bind proteins. As a result, we employ it to regulate the expression of our CRISPR regulatory system since, when combined with L7Ae, it suppresses the translation of the protein portion (Cas12g), Whenever there is a high quantity of phenylalanine as shown in figure 1.
Literature Characterization
In this study, Using comparative gel electrophoresis, When Kt-7 and Kt-23 undergo electrophoresis side by side in the presence of 2 mM Mg2+ ions, their mobility patterns are very comparable, indicating that they fold to the same extent under these circumstances.
References
1. Schroeder, K. T., & Lilley, D. M. (2009). Ion-induced folding of a kink turn that departs from the conventional sequence. Nucleic acids research, 37(21), 7281-7289. 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]