Difference between revisions of "Part:BBa K1051152"
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===principle=== | ===principle=== | ||
− | <p> | + | <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> |
+ | |||
+ | https://static.igem.org/mediawiki/2013/1/1f/Figure1.protein-import_pathways_for_mitochondrial_proteins.png | ||
+ | Fig. mit pathway | ||
+ | |||
===Results=== | ===Results=== | ||
− | + | ||
===Reference=== | ===Reference=== | ||
Acid, S. A. (2004). Lehninger principles of biochemistry | Acid, S. A. (2004). Lehninger principles of biochemistry |
Revision as of 13:16, 23 October 2013
GalI+H2A2+GFP+TYB
GalI+H2A2+GFP+TYB
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 150
Illegal AgeI site found at 652 - 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 1613
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.
Fig. mit pathway
Results
Reference
Acid, S. A. (2004). Lehninger principles of biochemistry