Rhodopsin, Gq and phospholipase C activation in cephalopod photoreceptors

被引：12

作者：

Bhatia, J ^{[1
]}

Davies, A ^{[1
]}

Gaudoin, JB ^{[1
]}

Saibil, HR ^{[1
]}

机构：

[1] UNIV LONDON BIRKBECK COLL,DEPT CRYSTALLOG,LONDON WC1E 7HX,ENGLAND

来源：

JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY | 1996年 / 35卷 / 1-2期

关键词：

rhodopsin; cephalopods; photoreceptors; G-protein; phospholipase C;

D O I：

10.1016/1011-1344(96)07309-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We present characterization of the rhodopsin, Gq and phosphatidylinositol-specific phospholipase C (PLC) from the signal transduction pathway of cephalopod photoreceptors. Cephalopod rhodopsins are unique in possessing a C-terminal extension of proline-rich repeats, and they have a strong tendency to form ordered arrays. Two-dimensional arrays of a full-length and C-terminally-truncated cephalopod rhodopsin have been obtained. The C termini appear to cluster the rhodopsins into small groups. An AIF(4)(-)-activated Gq alpha subunit has been isolated and shown to activate a partially purified PLC beta. This 130 kDa PLC, isolated by absorption on heparin agarose, showed a specific activity of 195 nmol of phosphatidylinositol 4,5-bisphosphate hydrolysed per milligram of protein per minute in the presence of 1.6 mu M free calcium.

引用

页码：19 / 23

页数：5

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