Difference between revisions of "Part:BBa K1642001"

Revision as of 12:17, 9 September 2015

Codon-optimized Halorhodopsin with His-tag

Halorhodopsin (HR) proteins are light-driven inward-directed chloride pumps from halobacteria. They are membrane-integral proteins of the rhodopsin superfamily that form a covalent bond with the carotenoid-derived chromophore all-trans retinal. Absorption of a photon with a defined optimal wavelength induces trans-cis isomerization of retinal, which triggers a catalytic photocycle of conformational changes in the protein, resulting in the net import of one chloride per photon into the cytoplasm.[1] And its electrophysiological properties have been characterized in Xenopus laevis oocytes.[2] We use it as our biodesalination driver which confers cyanobacteria the ability to absorb chloride to a significant degree.

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 NgoMIV site found at 133
Illegal NgoMIV site found at 292
Illegal NgoMIV site found at 613
Illegal AgeI site found at 484
1000
COMPATIBLE WITH RFC[1000]

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 __NOTOC__
 <partinfo>BBa_K1642001 short</partinfo>
-pHR
+Halorhodopsin (HR) proteins are light-driven inward-directed chloride pumps from halobacteria. They are membrane-integral proteins of the rhodopsin superfamily that form a covalent bond with the carotenoid-derived chromophore all-trans retinal. Absorption of a photon with a defined optimal wavelength induces trans-cis isomerization of retinal, which triggers a catalytic photocycle of conformational changes in the protein, resulting in the net import of one chloride per photon into the cytoplasm.[1] And its electrophysiological properties have been characterized in Xenopus laevis oocytes.[2] We use it as our biodesalination driver which confers cyanobacteria the ability to absorb chloride to a significant degree.
 <!-- Add more about the biology of this part here