Difference between revisions of "Part:BBa K243027"

Latest revision as of 17:30, 22 October 2009

His-FOS

This part is composed of a polyhistidine-tagged leucine zipper domain derived from the mammalian c-Fos protein. It can form DNA-binding homo- and heterodimers and can be used to target fused protein parts to specific DNA regions.

[http://www.rcsb.org/pdb/explore/images.do?structureId=1FOS Heterodimeric Fos complex]

Usage and Biology

Activator protein-1 (AP-1) is a crucial transcription factor implicated in numerous cancers and binds DNA as a dimer. Two classes of core DNA sequences, the sequences TRE (TGACTCA) and CRE (TGACGTCA), can be recognized by AP-1. Nine homologues of the AP-1 leucine zipper region have been characterized. All of them are able to form heterodimers, some also form homodimers. One of them is the so called c-Fos. Via their leucin zipper domains they interact with each other and bind DNA with their bipartite domain (Abate et al., Mol Cell Biol., 1991). The sequence for the bZip domains of c-Fos is linked to a His tag which allows protein purification using a Ni-NTA column. Soluble expression in Escherichia coli is possible.
In the research dimerized c-fos is normally used as a DNA binding molecule.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
INCOMPATIBLE WITH RFC[21]
Illegal BamHI site found at 19
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

@@ Line 2: / Line 2: @@
 <partinfo>BBa_K243027 short</partinfo><br>
-Activator protein-1 (AP-1) is a crucial transcription factor implicated in numerous cancers and binds DNA as a dimer. Two classes of core DNA sequences, the sequences TRE (TGACTCA) and CRE (TGACGTCA), can be recognized by AP-1. Nine homologues of the AP-1 leucine zipper region have been characterized. All of them are able to form heterodimers, some also form homodimers. One of them is the so called c-Fos. Via leucin zipper they interact among each other and with their bipartite domain they bind DNA. (Abate et al., Mol Cell Biol. 1991 July).
+This part is composed of a polyhistidine-tagged leucine zipper domain derived from the mammalian c-Fos protein. It can form DNA-binding homo- and heterodimers and can be used to target fused protein parts to specific DNA regions.
 <br>
 [[Image:1fos bio r 250.jpg]] <br>
@@ Line 10: / Line 10: @@
 ===Usage and Biology===
-The sequence for the bZip domains of c-Fos is linked to a His tag and allows the purification over a Ni-NTA column and the expression as soluble proteins in ''Escherichia coli''.<br>
+Activator protein-1 (AP-1) is a crucial transcription factor implicated in numerous cancers and binds DNA as a dimer. Two classes of core DNA sequences, the sequences TRE (TGACTCA) and CRE (TGACGTCA), can be recognized by AP-1. Nine homologues of the AP-1 leucine zipper region have been characterized. All of them are able to form heterodimers, some also form homodimers. One of them is the so called c-Fos. Via their leucin zipper domains they interact with each other and bind DNA with their bipartite domain (Abate et al., Mol Cell Biol., 1991). The sequence for the bZip domains of c-Fos is linked to a His tag which allows protein purification using a Ni-NTA column. Soluble expression in ''Escherichia coli'' is possible.<br>
 In the research dimerized c-fos is normally used as a DNA binding molecule.<br>