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Simple purification and functional reconstitution of octopus photoreceptor Gq, which couples rhodopsin to phospholipase C.

Abstract：

:In invertebrate photoreceptors, illuminated rhodopsin activates multiple G proteins, which are assumed to initiate multiple phototransduction cascades. In this paper, we focused on one of the phototransduction cascades, which utilizes rhodopsin, a Gq-like G protein, and phospholipase C (PLC). A Gq-like G protein from octopus photoreceptors was successfully purified to apparent homogeneity as an active form by simple two-step chromatography. The purified G protein had an alpha beta gamma-trimeric structure consisting of 44-kDa alpha, 37-kDa beta, and 9-kDa gamma subunits. The 44-kDa alpha subunit was assigned to the Gq class by western blot with antiserum against mammalian Gq alpha and by partial amino acid sequencing of its proteolytic fragments. Light-dependent binding of GTP gamma S was observed when the purified octopus Gq was reconstituted with octopus rhodopsin that had been integrated into phospholipid vesicles. Octopus Gq activated PLC beta 1 purified from bovine brain dose-dependently in the presence of A1F4-. Finally, light- and GTP-dependent activation of PLC beta 1 was observed in a reconstitution system consisting of octopus rhodopsin, Gq, and bovine PLC beta 1.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Kikkawa S,Tominaga K,Nakagawa M,Iwasa T,Tsuda M

doi

10.1021/bi961360v

subject

Has Abstract

pub_date

1996-12-10 00:00:00

pages

15857-64

issue

49

eissn

0006-2960

issn

1520-4995

pii

bi961360v

journal_volume

35

pub_type

杂志文章

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