Difference between revisions of "Part:BBa K1051152"
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===principle===
 
===principle===
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<p>Histones are nuclear proteins package DNA into nucleosomes, and they are responsible for maintaining the shape and structure of a nucleosome. One chromatin molecule is composed of at least one of each core histones per 100 base pairs of DNA.[The Nucleosome: From Genomic Organization to Genomic Regulation.] There are five families of histones known to date, termed H1/H5, H2A, H2B, H3, and H4. H2A is considered a core histone, along with H2B, H3 and H4. Core formation first occurs through the interaction of two H2A molecules(Acid, 2004). Then, H2A forms a dimer with H2B; the core molecule is complete when H3-H4 also attaches to form a tetramer.</p>
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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===
 
===Results===
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https://static.igem.org/mediawiki/2013/b/ba/Nucleus.jpg
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===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


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 150
    Illegal AgeI site found at 652
  • 1000
    INCOMPATIBLE 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.

Figure1.protein-import_pathways_for_mitochondrial_proteins.png Fig. mit pathway

Results

Reference

Acid, S. A. (2004). Lehninger principles of biochemistry