Difference between revisions of "Part:BBa K2549012"

Revision as of 05:13, 7 October 2018

ZF21.16 split C

This part is the C-terminal fragment of the zinc finger. Amino acid residues of the recognition helices for three-finger arrays are substituted by the reported synthetic zinc finger 21.16 residues^[1] on the basis of the BCR_ABL-1 artificial zinc finger. Splicing site between the 48 and 49 residues is chosen as is reported to function the second highest among the tested 12 splicing sites^[2]. This site is chosen as the +1 position residue for the CfaC (Part:BBa_K2549010) has to be a cysteine^[3]. It was fused to the CfaC (Part:BBa_K2549010) intein. When (ZF-N + CfaN Part:BBa_K2549009) co-expressed with (CfaC Part:BBa_K2549010 + ZF-C) the DNA binding activity of the ZF will be restored.

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]

Usage and Biology

TBA

References

↑ A synthetic biology framework for programming eukaryotic transcription functions. Khalil AS, Lu TK, Bashor CJ, ..., Joung JK, Collins JJ. Cell, 2012 Aug;150(3):647-58 PMID: 22863014; DOI: 10.1016/j.cell.2012.05.045
↑ A tunable zinc finger-based framework for Boolean logic computation in mammalian cells. Lohmueller JJ, Armel TZ, Silver PA. Nucleic Acids Res, 2012 Jun;40(11):5180-7 PMID: 22323524; DOI: 10.1093/nar/gks142
↑ A promiscuous split intein with expanded protein engineering applications. Stevens AJ, Sekar G, Shah NH, ..., Cowburn D, Muir TW. Proc Natl Acad Sci U S A, 2017 Aug;114(32):8538-8543 PMID: 28739907; DOI: 10.1073/pnas.1701083114

[1] A synthetic biology framework for programming eukaryotic transcription functions. Khalil AS, Lu TK, Bashor CJ, ..., Joung JK, Collins JJ. Cell, 2012 Aug;150(3):647-58 PMID: 22863014; DOI: 10.1016/j.cell.2012.05.045

[2] A tunable zinc finger-based framework for Boolean logic computation in mammalian cells. Lohmueller JJ, Armel TZ, Silver PA. Nucleic Acids Res, 2012 Jun;40(11):5180-7 PMID: 22323524; DOI: 10.1093/nar/gks142

[3] A promiscuous split intein with expanded protein engineering applications. Stevens AJ, Sekar G, Shah NH, ..., Cowburn D, Muir TW. Proc Natl Acad Sci U S A, 2017 Aug;114(32):8538-8543 PMID: 28739907; DOI: 10.1073/pnas.1701083114

[1]

[2]

[3]

@@ Line 2: / Line 2: @@
 <partinfo>BBa_K2549012 short</partinfo>
-This part is the C-terminal fragment of the zinc finger. Amino acid residues of the recognition helices for three-finger arrays are substituted by the reported synthetic zinc finger 21.16 residues<ref>A synthetic biology framework for programming eukaryotic transcription functions. Khalil AS, Lu TK, Bashor CJ, ..., Joung JK, Collins JJ. Cell, 2012 Aug;150(3):647-58 PMID: 22863014; DOI: 10.1016/j.cell.2012.05.045</ref> on the basis of the BCR_ABL-1 artificial zinc finger[2]. Splicing site between the 48 and 49 residues is chosen as is reported to function the second highest among the tested 12 splicing sites<ref>A tunable zinc finger-based framework for Boolean logic computation in mammalian cells. Lohmueller JJ, Armel TZ, Silver PA. Nucleic Acids Res, 2012 Jun;40(11):5180-7 PMID: 22323524; DOI: 10.1093/nar/gks142</ref>. This site is chosen as the +1 position residue for the CfaC ([[Part:BBa_K2549010]]) has to be a cysteine<ref>A promiscuous split intein with expanded protein engineering applications. Stevens AJ, Sekar G, Shah NH, ..., Cowburn D, Muir TW. Proc Natl Acad Sci U S A, 2017 Aug;114(32):8538-8543 PMID: 28739907; DOI: 10.1073/pnas.1701083114</ref>. It was fused to the CfaC ([[Part:BBa_K2549010]]) intein. When (ZF-N + CfaN [[Part:BBa_K2549009]]) co-expressed with (CfaC [[Part:BBa_K2549010]] + ZF-C) the DNA binding activity of the ZF will be restored.
+This part is the C-terminal fragment of the zinc finger. Amino acid residues of the recognition helices for three-finger arrays are substituted by the reported synthetic zinc finger 21.16 residues<ref>A synthetic biology framework for programming eukaryotic transcription functions. Khalil AS, Lu TK, Bashor CJ, ..., Joung JK, Collins JJ. Cell, 2012 Aug;150(3):647-58 PMID: 22863014; DOI: 10.1016/j.cell.2012.05.045</ref> on the basis of the BCR_ABL-1 artificial zinc finger. Splicing site between the 48 and 49 residues is chosen as is reported to function the second highest among the tested 12 splicing sites<ref>A tunable zinc finger-based framework for Boolean logic computation in mammalian cells. Lohmueller JJ, Armel TZ, Silver PA. Nucleic Acids Res, 2012 Jun;40(11):5180-7 PMID: 22323524; DOI: 10.1093/nar/gks142</ref>. This site is chosen as the +1 position residue for the CfaC ([[Part:BBa_K2549010]]) has to be a cysteine<ref>A promiscuous split intein with expanded protein engineering applications. Stevens AJ, Sekar G, Shah NH, ..., Cowburn D, Muir TW. Proc Natl Acad Sci U S A, 2017 Aug;114(32):8538-8543 PMID: 28739907; DOI: 10.1073/pnas.1701083114</ref>. It was fused to the CfaC ([[Part:BBa_K2549010]]) intein. When (ZF-N + CfaN [[Part:BBa_K2549009]]) co-expressed with (CfaC [[Part:BBa_K2549010]] + ZF-C) the DNA binding activity of the ZF will be restored.
 <span class='h3bb'>Sequence and Features</span>