Identification of Gα11 as the phospholipase C-activating G-protein of turkey erythrocytes

D. H. Maurice, G. L. Waldo, A. J. Morris, R. A. Nicholas, T. K. Harden

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33 Scopus citations

Abstract

A 43 kDa phospholipase C-activating protein has been purified previously from turkey erythrocytes and shown to express immunological properties expected of that of the G(q) family of G-protein α-subunits [Waldo, Boyer, Morris and Harden (1991) J. Biol. Chem. 266, 14217-14225]. Internal amino acid sequence has now been obtained from this protein which shares 50-100 % sequence identity with sequences encoded by mammalian Gα11 and Gα(q) cDNAs. To identify the purified protein unambiguously, it was necessary to compare its amino acid sequence with the sequence encoded by avian G-protein α-subunit cDNA. As such, mouse Gα(q) was used as a probe to screen turkey brain and fetal-turkey blood cDNA libraries. A full-length cDNA was identified that encodes avian Gα11, on the basis of its 96-98 % amino acid identity with mammalian Gα(π). All eight peptides sequenced from the turkey erythrocyte phospholipase C-activating protein are completely contained within the deduced amino acid sequence of the avian Gα(11) cDNA. Expression of this cDNA in Sf9 cells by using a baculovirus expression system resulted in the production of a 43 kDa protein that reacts strongly with antisera to the G(q) family of G-protein α-subunits and activated purified avian phospholipase C in an AlF-4-dependent manner. Taken together, these results unambiguously identify the protein purified from turkey erythrocytes, on the basis of its capacity to activate avian phospholipase C, as Gα(π).

Original languageEnglish
Pages (from-to)765-770
Number of pages6
JournalBiochemical Journal
Volume290
Issue number3
DOIs
StatePublished - 1993

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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