Difference between revisions of "Part:BBa K3504002"

(Usage)
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==Usage==
 
==Usage==
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∼60kDa nsP3 : The functional role of the nsP3 hasn’t been clear throughout history. It still has a primary part in the RNA synthesis as mutations in nsP3 exhibited defects in the start of minus-strand synthesis or subgenomic RNA synthesis. The alphavirus nsP3 protein has three recognized domains: the macrodomain, the alphavirus unique domain (AUD) and the hypervariable region. The macrodomains of CHIKV and VEEV were found to bind to DNA, RNA and polyADP-ribose in addition to exhibiting adenosine diphosphoribose 1′-phosphate phosphatase activity. Genetic manipulations within the AUD have resulted in defects in minus-strand and subgenomic RNA synthesis, polyprotein processing, and neurovirulence where the exact mechanism is not identified up till now. The C-terminal domain of nsP3 is characterized as being hypervariable and this hypervariable domain is shown to be responsible for the formation of virus-species specific complexes in infected cells. At this time it is not clear that the identified interactions of nsP3 with host factors influence viral RNA synthesis or whether they are indicative of another nsP3 function that regulates the host cell environment.
 +
 
==Characterization==
 
==Characterization==
 
==Improvements==
 
==Improvements==

Revision as of 11:26, 12 October 2020


nSP3-Eastern equine encephalitis virus

Part Description

Nsp3 is one of four non structural proteins that together forms the main complex responsible for the synthesis positive-sense viral RNAs, results in the synthesis of both the genomic and subgenomic RNAs, of which the subgenomic RNA is produced in excess of the viral genome. Which allows the virus to self-replicate into millions of copies of the virus.

Usage

∼60kDa nsP3 : The functional role of the nsP3 hasn’t been clear throughout history. It still has a primary part in the RNA synthesis as mutations in nsP3 exhibited defects in the start of minus-strand synthesis or subgenomic RNA synthesis. The alphavirus nsP3 protein has three recognized domains: the macrodomain, the alphavirus unique domain (AUD) and the hypervariable region. The macrodomains of CHIKV and VEEV were found to bind to DNA, RNA and polyADP-ribose in addition to exhibiting adenosine diphosphoribose 1′-phosphate phosphatase activity. Genetic manipulations within the AUD have resulted in defects in minus-strand and subgenomic RNA synthesis, polyprotein processing, and neurovirulence where the exact mechanism is not identified up till now. The C-terminal domain of nsP3 is characterized as being hypervariable and this hypervariable domain is shown to be responsible for the formation of virus-species specific complexes in infected cells. At this time it is not clear that the identified interactions of nsP3 with host factors influence viral RNA synthesis or whether they are indicative of another nsP3 function that regulates the host cell environment.

Characterization

Improvements

Sequence and Features


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal PstI site found at 426
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 1297
    Illegal PstI site found at 426
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal XhoI site found at 1461
    Illegal XhoI site found at 1522
    Illegal XhoI site found at 1563
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal PstI site found at 426
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal PstI site found at 426
    Illegal AgeI site found at 1002
    Illegal AgeI site found at 1371
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI site found at 1560
    Illegal BsaI site found at 1578
    Illegal BsaI.rc site found at 1087