Difference between revisions of "Part:BBa K208002"

Revision as of 16:12, 22 October 2009

Gene III Signal Peptide - Silver Fusion Compatible

This is a Silver-fusion compatible BioBrick part that can be attached to other proteins to target those proteins for export out of the cytoplasm. The GeneIII sequence targets unfolded proteins to the Sec-dependent pathway of Type II secretion.

Usage and Biology

Signal peptides consist of about 15-30 amino acids and are generally required to direct a secretory protein to the translocons of the cytoplasmic membrane (Pugsley, 1993; Choi, 2004; Luirink, 2004). Despite overall sequence variability, structural similarities exist between different signal peptides, including a positively-charged 2-10 amino acid N-region, a hydrophobic core H-region, and a neutral C-domain of about 6 residues (Pugsley, 1993; Molhoj, 2004; Berks, 2000). The C-domain conforms to the -3, -1 rule in which amino acids with short and neutral side-chains, such as alanine, are required in positions -3 and -1 of the sequence (Choi, 2004; von Heijne, 1984). A signal peptidase interacts with a cleavage recognition site within the C-domain to release the protein into the periplasmic space (Luiritz, 2004; Choi, 2004). Once in the periplasm, secretion into the extracellular media can occur via the action of a secreton, or by chemical or enzymatic methods.

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
COMPATIBLE WITH RFC[1000]

@@ Line 2: / Line 2: @@
 <partinfo>BBa_K208002 short</partinfo>
-GeneIII secretion tag
+This is a Silver-fusion compatible BioBrick part that can be attached to other proteins to target those proteins for export out of the cytoplasm. The GeneIII sequence  targets unfolded proteins to the Sec-dependent pathway of Type II secretion.
-<!-- Add more about the biology of this part here
 ===Usage and Biology===
+Signal peptides consist of about 15-30 amino acids and are generally required to direct a secretory protein to the translocons of the cytoplasmic membrane (Pugsley, 1993; Choi, 2004; Luirink, 2004). Despite overall sequence variability, structural similarities exist between different signal peptides, including a positively-charged 2-10 amino acid N-region, a hydrophobic core H-region, and a neutral C-domain of about 6 residues (Pugsley, 1993; Molhoj, 2004; Berks, 2000). The C-domain conforms to the -3, -1 rule in which amino acids with short and neutral side-chains, such as alanine, are required in positions -3 and -1 of the sequence (Choi, 2004; von Heijne, 1984). A signal peptidase interacts with a cleavage recognition site within the C-domain to release the protein into the periplasmic space (Luiritz, 2004; Choi, 2004). Once in the periplasm, secretion into the extracellular media can occur via the action of a secreton, or by chemical or enzymatic methods.
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