Difference between revisions of "Part:BBa K1639008"

(Created page with "__NOTOC__ <partinfo>BBa_K1639008 short</partinfo> TEV protease (also called Tobacco Etch Virus nuclear inclusion a endopeptidase) is a highly sequence-specific cysteine protease...")
 
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TEV protease (also called Tobacco Etch Virus nuclear inclusion a endopeptidase) is a highly sequence-specific cysteine protease from Tobacco Etch Virus (TEV).The consensus for these native cut sites is '''ENLYFQ\S''' where ‘\’ denotes the cleaved peptide bond.One of the main uses of this protein is for removing affinity tags from purified proteins. The reason for the use of TEV protease as a biochemical tool is its '''high sequence specificity'''. This specificity allows for the controlled cleavage of proteins when the preference sequence is inserted into flexible loops. It also makes it relatively non-toxic in vivo as the recognized sequence scarcely occurs in proteins.[1]
 
TEV protease (also called Tobacco Etch Virus nuclear inclusion a endopeptidase) is a highly sequence-specific cysteine protease from Tobacco Etch Virus (TEV).The consensus for these native cut sites is '''ENLYFQ\S''' where ‘\’ denotes the cleaved peptide bond.One of the main uses of this protein is for removing affinity tags from purified proteins. The reason for the use of TEV protease as a biochemical tool is its '''high sequence specificity'''. This specificity allows for the controlled cleavage of proteins when the preference sequence is inserted into flexible loops. It also makes it relatively non-toxic in vivo as the recognized sequence scarcely occurs in proteins.[1]
  
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PotB59, chimeric protein that is formed by the N-terminal region of PomB and the C-terminal of ''E. Coli'' MotB
 
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It was shown that a chimeric protein, PotB, renamed as PotB59, that has the N-terminal region of PomB (1–50) fused to the C-terminal periplasmic region of ''E. coli'' MotB (59–308), is functional with PomA in ''E. coli'' as well as in strains of ''V. alginolyticus'' that are defective in MotX or MotY (Asai et al. 2003) Instead of the hydrogen-dependent MotA, MotB stator protein partially adapted from the ''V. alginolyticus,'' sodium-dependent Stator proteins were insalled. After this adaptation, the flagellar velocity increased by twice fold.
 
  
 
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Revision as of 13:34, 13 September 2015

Tev Protease, single S219V mutation in the internal cleavage site

TEV protease (also called Tobacco Etch Virus nuclear inclusion a endopeptidase) is a highly sequence-specific cysteine protease from Tobacco Etch Virus (TEV).The consensus for these native cut sites is ENLYFQ\S where ‘\’ denotes the cleaved peptide bond.One of the main uses of this protein is for removing affinity tags from purified proteins. The reason for the use of TEV protease as a biochemical tool is its high sequence specificity. This specificity allows for the controlled cleavage of proteins when the preference sequence is inserted into flexible loops. It also makes it relatively non-toxic in vivo as the recognized sequence scarcely occurs in proteins.[1]


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 2
    Illegal XhoI site found at 744
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI site found at 605