Difference between revisions of "Part:BBa K1150002"
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Krüppel-associated Box repressor domains - commonly termed as KRAB - are highly conserved polypeptide motifs and were first functionally characterized in 1991 (<i>Rosati et al.</i>, 1991). As they constitute about one third of all human zinc finger transcription factors, key regulatory features in higher eukaryotic transcriptomics are suggested (<i>Witzgall et al.</i>, 1994). Even in terms of tetrapod evolution, the role of their great abundance has been extensively discussed (<i>Birtle & Ponting</i>, 2006). Even though KRAB minimal domains are usually no longer than ~ 50-75 amino acids, their mechanism of function remains complex. <br><br> Common biochemical models suggest a key role in epigenetic silencing, by recruiting a scaffold of diverse proteins - amongst others histone deacetylases and histone methyltransferases (<i>Urrutia</i>, 2003). Til date in 2013, KRAB repressor domains were attached to several DNA binding proteins such as tetR, TAL effectors and [http://2013.igem.org/Team:Freiburg/Project/effector#repression dCas9] - thereby efficiently silencing gene expression downstream of desired target promoters. | Krüppel-associated Box repressor domains - commonly termed as KRAB - are highly conserved polypeptide motifs and were first functionally characterized in 1991 (<i>Rosati et al.</i>, 1991). As they constitute about one third of all human zinc finger transcription factors, key regulatory features in higher eukaryotic transcriptomics are suggested (<i>Witzgall et al.</i>, 1994). Even in terms of tetrapod evolution, the role of their great abundance has been extensively discussed (<i>Birtle & Ponting</i>, 2006). Even though KRAB minimal domains are usually no longer than ~ 50-75 amino acids, their mechanism of function remains complex. <br><br> Common biochemical models suggest a key role in epigenetic silencing, by recruiting a scaffold of diverse proteins - amongst others histone deacetylases and histone methyltransferases (<i>Urrutia</i>, 2003). Til date in 2013, KRAB repressor domains were attached to several DNA binding proteins such as tetR, TAL effectors and [http://2013.igem.org/Team:Freiburg/Project/effector#repression dCas9] - thereby efficiently silencing gene expression downstream of desired target promoters. | ||
| − | [[File:KRAB_Figure_Freiburg.jpg| | + | [[File:KRAB_Figure_Freiburg.jpg|200px|"Fig. 1" Structural Mechanism of KRAB Transcription Factors, as suggested by Urrutia, R. (2003).]]<br><br><br><br><br> |
Revision as of 16:58, 27 September 2013
KRAB
| KRAB | |
|---|---|
| Function | Repressor domain |
| Use in | Mammalian cells |
| RFC standard | RFC 25 |
| Backbone | pSB1C3 |
| Organism | Homo sapiens |
| Source | Konrad Müller, pKM102 |
| Submitted by | [http://2013.igem.org/Team:Freiburg Freiburg 2013] |
Krüppel-associated Box repressor domains - commonly termed as KRAB - are highly conserved polypeptide motifs and were first functionally characterized in 1991 (Rosati et al., 1991). As they constitute about one third of all human zinc finger transcription factors, key regulatory features in higher eukaryotic transcriptomics are suggested (Witzgall et al., 1994). Even in terms of tetrapod evolution, the role of their great abundance has been extensively discussed (Birtle & Ponting, 2006). Even though KRAB minimal domains are usually no longer than ~ 50-75 amino acids, their mechanism of function remains complex.
Common biochemical models suggest a key role in epigenetic silencing, by recruiting a scaffold of diverse proteins - amongst others histone deacetylases and histone methyltransferases (Urrutia, 2003). Til date in 2013, KRAB repressor domains were attached to several DNA binding proteins such as tetR, TAL effectors and [http://2013.igem.org/Team:Freiburg/Project/effector#repression dCas9] - thereby efficiently silencing gene expression downstream of desired target promoters.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 244
Illegal SapI.rc site found at 208