Difference between revisions of "Part:BBa K1051130"

 
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<partinfo>BBa_K1051130 short</partinfo>
 
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<partinfo>BBa_K1051130 parameters</partinfo>
 
<partinfo>BBa_K1051130 parameters</partinfo>
 
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===principle===
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<p>Though it accounts a small ratio in the cell space, mitochondria possess about 10% to 15% proteins encoded by nuclear genes in eukaryotic organisms. These proteins are synthesized in cytosol and then recognized by the membrane receptors of mitochondria. Translocases in the outer and inner membrane of mitochondria mediate the import and intra-mitochondrial sorting of these proteins. ATP is used as an energy source; Chaperones and auxiliary factors assist in folding and assembly of mitochondrial proteins into their native, three-dimensional structures. 　　As shown in the figure above, beta-barrel outer-membrane proteins (dark green), precursor proteins (brown) with positively charged amino-terminal presequences and multispanning inner-membrane proteins (blue) with internal targeting signals are recognized by specific receptors of the outer mitochondrial membrane (TOM) translocases Tom20, Tom22 and/or Tom70. The precursor proteins are then translocated through a small Tom proteins of the TOM complex, Tom40 pore, which the TOM complex contains two or three.</p>
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https://static.igem.org/mediawiki/2013/1/1f/Figure1.protein-import_pathways_for_mitochondrial_proteins.png
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Fig. mit pathway
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===Results===
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===Reference===
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Nature Reviews Molecular Cell Biology 5, 519-530 (July 2004) | doi:10.1038/nrm142 Mitochondrial import and the twin-pore translocase

Latest revision as of 13:05, 23 October 2013

GFP+TOM40

GFP+TOM40(C terminal)

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
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 644
    Illegal SapI site found at 853


principle

Though it accounts a small ratio in the cell space, mitochondria possess about 10% to 15% proteins encoded by nuclear genes in eukaryotic organisms. These proteins are synthesized in cytosol and then recognized by the membrane receptors of mitochondria. Translocases in the outer and inner membrane of mitochondria mediate the import and intra-mitochondrial sorting of these proteins. ATP is used as an energy source; Chaperones and auxiliary factors assist in folding and assembly of mitochondrial proteins into their native, three-dimensional structures. 　　As shown in the figure above, beta-barrel outer-membrane proteins (dark green), precursor proteins (brown) with positively charged amino-terminal presequences and multispanning inner-membrane proteins (blue) with internal targeting signals are recognized by specific receptors of the outer mitochondrial membrane (TOM) translocases Tom20, Tom22 and/or Tom70. The precursor proteins are then translocated through a small Tom proteins of the TOM complex, Tom40 pore, which the TOM complex contains two or three.

Figure1.protein-import_pathways_for_mitochondrial_proteins.png Fig. mit pathway

Results

Reference

Nature Reviews Molecular Cell Biology 5, 519-530 (July 2004) | doi:10.1038/nrm142 Mitochondrial import and the twin-pore translocase