The 35- and 36-kDa β subunits of GTP-binding regulatory proteins are products of separate genes

T. T. Amatruda, N. Gautam, H. K.W. Fong, J. K. Northup, M. I. Simon

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46 Scopus citations

Abstract

The wide range of functions attributed to GTP-binding regulatory proteins (G proteins) is reflected in the structural diversity which exists among the α, β, and γ subunits of G proteins. Recently two cDNA clones encoding β subunits, β1 and β2, were isolated from bovine and human cDNA libraries. We report here that the β2 gene encodes the 35-kilodalton (kDa) component of the β3536 subunit of G proteins and that the β1 gene encodes the 36-kilodalton component. The in vitro translation product of the β2 cDNA co-migrates with the 35-kDa β subunit (β35), while the in vitro product of the β1 cDNA co-migrates with the 36-kDa β subunit (β36) on denaturing polyacrylamide gels. In addition, antisera generated against synthetic β2 peptides bind specifically to the β35 component of isolated G proteins and to a 35-kDa protein in myeloid cell membranes. Our results suggest that the two β subunits could serve distinct functions, as they are derived from separate genes which have been highly conserved in evolution.

Original languageEnglish
Pages (from-to)5008-5011
Number of pages4
JournalJournal of Biological Chemistry
Volume263
Issue number11
StatePublished - Jan 1 1988
Externally publishedYes

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    Amatruda, T. T., Gautam, N., Fong, H. K. W., Northup, J. K., & Simon, M. I. (1988). The 35- and 36-kDa β subunits of GTP-binding regulatory proteins are products of separate genes. Journal of Biological Chemistry, 263(11), 5008-5011.