Plasmid 25867: qz5

• Gene/insert name: Gq alpha
• Alt name: G protein alpha subunit
• Alt name: Gnaq
• Species: M. musculus (mouse)
• Entrez Gene: Gnaq (1110005L02Rik, 6230401I02Rik, AA408290, AW060788, Dsk1, Dsk10, Galphaq, Gq, GqI)
  
• Fusion protein or tag: HA (see comments)
• Mutation: Replacement of the five carboxyl-terminal amino acids of Gq alpha (EYNLV) with those of Gz alpha(YIGLC)
• Vector backbone: pcDNA1
  (Search Vector Database)
• Vector type: Mammalian Expression
• Backbone size w/o insert (bp): 4000
• Cloning site 5': BamHI
• Site destroyed during cloning: Unknown
• Cloning site 3': NsiI
• Site destroyed during cloning: Unknown
• 5' sequencing primer: CMV-F
• 3' sequencing primer: SP6
• Bacterial resistance(s) Ampicillin and Tetracycline
• Growth strain(s) Top10/P3
• Growth temperature (℃): 37
• Growth instructions: Plasmid contains SupF. Grow in TOP10/P3 cells.
• High or low copy: Unknown
• Sequence: View sequences (3)
• Supplemental document: G-protein chimera user manual (application/pdf)
• Principal Investigator: Bruce Conklin
• Terms and Licenses: MTA

Comments: 

This is Gq alpha with the C-terminal amino acids changed from Gq alpha to Gz alpha residues (EYNLV to YIGLC). Works the same as qi5 and is the least popular since no one knows what Gz alpha really does in nature. Since qz5 is not sensitive to pertussis toxin, qz5 may be the only G protein activated by a Gi-coupled receptor in cells treated with pertussis toxin. This trick can be experimentally useful in settings where you want experimental control of the exact G protein and the receptor that is activated. It is theoretically possible that this construct will work better than the other constructs for particular receptors, but the Conklin lab has not seen this happen yet.

Contains an internal hemaglutinin epitope tag (DVPDYA) that has no effect on receptor coupling.

Please see supplemental document for G-protein chimera user manual.

Article: Substitution of three amino acids switches receptor specificity of Gq alpha to that of Gi alpha. Conklin et al (Nature. 1993 May 20. 363(6426):274-6. PubMed)