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Functional heterogeneity of transducin α subunits
Author(s) -
Neubert Thomas A,
Hurley James B
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00037-4
Subject(s) - transducin , gtp' , glycine , chemistry , g protein , biochemistry , biology , amino acid , enzyme , signal transduction
The N‐terminal glycine of transducin α subunits is acylated by lauroyl (C12:0), myristoyl (C14:0), ( cis ‐Δ 5 )‐tetradecaenoyl (C14:1) or ( cis , cis ‐Δ 5 ,Δ 8 )‐tetradecadienoyl (C14:2) fatty acyl groups. We examined functional heterogeneity of transducin by sequentially eluting it from bleached outer segments using increasing concentrations of GTP then identifying the N‐terminal acyl groups on the eluted α subunits. C14:2 acylated transducin eluted at low GTP concentrations followed by C12:0, C14:1 and C14:0 transducin at higher GTP concentrations. This suggests functional heterogeneity in the different forms of transducin α subunits.