Difference between revisions of "Part:BBa K4140015"

(Usage)
(Usage)
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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==
(k-turn)a common structural motif identified in functioning RNA species. It typically consists of a tandem trans sugar edge-Hoogsteen G followed by a three-nucleotide bulge. 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
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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.  
We use it to control the expression of our regulatory system CRISPR as it inhibits translation of its protein part (cas12g) after combination with L7Ae. this happens in case of high level of phenylalanine.
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==Literature Characterization==
 
==Literature Characterization==

Revision as of 10:02, 29 September 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.  

Literature Characterization

Figure 1.Substrate RNA cleavage assay using wild-type and mutant target RNAs.





























References

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]