Kaguya-Taketori: /* Members */
[[File:2A peptide Working Mechanism.png.jpg|thumb|An illustration of 2A peptide function: when the [[Coding DNA sequence|CDS]] of a 2A peptide is inserted between two CDSs of protein, the peptide will be cleaved into two proteins folding independently.]]
'''2A self-cleaving peptides''', or '''2A peptides''', are a class of 18–22 [[amino acid|aa]]-long peptides being able to induce the cleaving of the [[recombinant protein]] in cell. 2A peptides are derived from the 2A region in the [[genome]] of [[virus]].<ref name="LiuChen2017"></ref><ref name="KarunaSudipto2010"></ref>
The members of 2A peptides are named after the virus in which they have been first described. For example, F2A, the first described 2A peptide, is derived from [[foot-and-mouth disease virus]]. <ref name="LiuChen2017"/>
==Members==
Four members of 2A peptides family are frequently used in life science research. They are P2A, E2A, F2A and T2A. F2A is derived from [[foot-and-mouth disease virus]] 18; E2A is derived from equine rhinitis A virus; P2A is derived from [[porcine teschovirus]]-1 2A; T2A is derived fromthosea asigna virus 2A. <ref name="LiuChen2017"/>
The following table shows the sequences of four members of 2A peptides. Adding the sequence “[[Glycine|G]][[Serine|S]][[Glycine|G]]” (Gly-Ser-Gly) on the N-terminal of a 2A peptide is optional. <ref name="Szymczak-WorkmanVignali2012"/>
{| class="wikitable"
|-
! Name !! Sequence
|-
| T2A || (GSG) E G R G S L L T C G D V E E N P G P
|-
| P2A || (GSG) A T N F S L L K Q A G D V E E N P G P
|-
| E2A || (GSG) Q C T N Y A L L K L A G D V E S N P G P
|-
| F2A || (GSG) V K Q T L N F D L L K L A G D V E S N P G P
|}
==Description==
The 2A-peptide-mediated cleavage commences after the [[Translation (biology)|translation]]. The cleavage is trigged by breaking of [[peptide bond]] between the [[Proline]] (P) and [[Glycine]] (G) in C-terminal of 2A peptide. The exact molecular mechanism of 2A-peptide-mediated cleavage is still unknown.<ref name="WangWang2015"></ref><ref></ref>
==Application==
In [[genetic engineering]], the 2A peptides are used to cleave a longer peptide into two shorter peptides. The 2A peptides can be applied when the fused protein doesn’t work. Inserting the [[Coding DNA sequence|CDS]] of a 2A peptide into the fusing point or replacing the linker sequence with the CDS of a 2A peptide protein can cleave the fused protein into two separated peptides, making the two peptides to regain the function.<ref name="Szymczak-WorkmanVignali2012"></ref>
2A peptides, when combined with the [[Internal ribosome entry site|IRES]] elements, can make it possible to generate three separated peptides within a single [[transcript]].<ref name="LiuChen2017"/>
==See Also==
*[[Internal ribosome entry site|IRES]]
*[[Recombinant DNA]]
==References==
[[Category:Genetic engineering]]
[[Category:Molecular biology]]
'''2A self-cleaving peptides''', or '''2A peptides''', are a class of 18–22 [[amino acid|aa]]-long peptides being able to induce the cleaving of the [[recombinant protein]] in cell. 2A peptides are derived from the 2A region in the [[genome]] of [[virus]].<ref name="LiuChen2017"></ref><ref name="KarunaSudipto2010"></ref>
The members of 2A peptides are named after the virus in which they have been first described. For example, F2A, the first described 2A peptide, is derived from [[foot-and-mouth disease virus]]. <ref name="LiuChen2017"/>
==Members==
Four members of 2A peptides family are frequently used in life science research. They are P2A, E2A, F2A and T2A. F2A is derived from [[foot-and-mouth disease virus]] 18; E2A is derived from equine rhinitis A virus; P2A is derived from [[porcine teschovirus]]-1 2A; T2A is derived fromthosea asigna virus 2A. <ref name="LiuChen2017"/>
The following table shows the sequences of four members of 2A peptides. Adding the sequence “[[Glycine|G]][[Serine|S]][[Glycine|G]]” (Gly-Ser-Gly) on the N-terminal of a 2A peptide is optional. <ref name="Szymczak-WorkmanVignali2012"/>
{| class="wikitable"
|-
! Name !! Sequence
|-
| T2A || (GSG) E G R G S L L T C G D V E E N P G P
|-
| P2A || (GSG) A T N F S L L K Q A G D V E E N P G P
|-
| E2A || (GSG) Q C T N Y A L L K L A G D V E S N P G P
|-
| F2A || (GSG) V K Q T L N F D L L K L A G D V E S N P G P
|}
==Description==
The 2A-peptide-mediated cleavage commences after the [[Translation (biology)|translation]]. The cleavage is trigged by breaking of [[peptide bond]] between the [[Proline]] (P) and [[Glycine]] (G) in C-terminal of 2A peptide. The exact molecular mechanism of 2A-peptide-mediated cleavage is still unknown.<ref name="WangWang2015"></ref><ref></ref>
==Application==
In [[genetic engineering]], the 2A peptides are used to cleave a longer peptide into two shorter peptides. The 2A peptides can be applied when the fused protein doesn’t work. Inserting the [[Coding DNA sequence|CDS]] of a 2A peptide into the fusing point or replacing the linker sequence with the CDS of a 2A peptide protein can cleave the fused protein into two separated peptides, making the two peptides to regain the function.<ref name="Szymczak-WorkmanVignali2012"></ref>
2A peptides, when combined with the [[Internal ribosome entry site|IRES]] elements, can make it possible to generate three separated peptides within a single [[transcript]].<ref name="LiuChen2017"/>
==See Also==
*[[Internal ribosome entry site|IRES]]
*[[Recombinant DNA]]
==References==
[[Category:Genetic engineering]]
[[Category:Molecular biology]]
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