Coding

Part:BBa_K1051116

Designed by: Jinchun Zhang   Group: iGEM13_Shenzhen_BGIC_ATCG   (2013-07-12)
Revision as of 17:11, 27 September 2013 by Yishion (Talk | contribs)

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Actin Targeting Protein

After added with 23 prefix and suffix, it can be used as a transporter to the actin of baking yeast. Also, when joining with different flourescent proteins, they can light the inner membrane using such proteins.


Sequence and Features


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal XbaI site found at 1432
    Illegal PstI site found at 311
    Illegal PstI site found at 1544
    Illegal PstI site found at 1634
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal PstI site found at 311
    Illegal PstI site found at 1544
    Illegal PstI site found at 1634
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal XhoI site found at 33
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal XbaI site found at 1432
    Illegal PstI site found at 311
    Illegal PstI site found at 1544
    Illegal PstI site found at 1634
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal XbaI site found at 1432
    Illegal PstI site found at 311
    Illegal PstI site found at 1544
    Illegal PstI site found at 1634
    Illegal AgeI site found at 142
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI site found at 1741
    Illegal SapI.rc site found at 1393


principle

In yeast, the cortical actin cytoskeleton seems to specify sites of growth of the cell surface. Because the actin-binding protein ABP1p is associated with the cortical cytoskeleton of Saccharomyces cerevisiae, it might be involved in the spatial organization of cell surface growth. ABP1p is localized to the cortical cytoskeleton and its overproduction causes assembly of the cortical actin cytoskeleton at inappropriate sites on the cell surface, resulting in delocalized surface growth. ABP1p is a novel protein with a 50 amino-acid C-terminal domain, which is very similar to the SH3 domain in the non-catalytic region of nonreceptor tyrosine kinases (including those encoded by the proto-oncogenes c-src and c-abl), in phospholipase C gamma and in alpha-spectrin. They also identified an SH3-related motif in the actin-binding tail domain of myosin-I. The identification of SH3 domains in a family of otherwise unrelated proteins that associate with the membrane cytoskeleton indicates that this domain might serve to bring together signal transduction proteins and their targets or regulators, or both, in the membrane cytoskeleton (Drubin, Mulholland, Zhu, & Botstein, 1990; Khorasanizadeh, 2004).

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Categories
Parameters
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