Particle-bound phytochrome : Differential pigment release by surfactants, ribonuclease and phospholipase C
スポンサーリンク
概要
- 論文の詳細を見る
Surfactants and hydrolytic enzymes were used to probe the nature of the constituent(s) to which phytochrome binds in particulate fractions from red-irradiated Cucurbita. [^<14>C]-choline and [^3H]-uridine pre-labelled tissue was used to monitor the release of phospholipids and RNA by these agents. Ribonuclease (RNase) digestion of 20,000 × g pellets eliminates both the phytochrome and ribonucleoprotein (RNP) which cosediment at 31S. Little [^<14>C]-choline occurs in the 31S fraction and the amount is not changed by RNase digestion. This is further evidence that phytochrome binds directly to the RNP in the 31S fraction rather than to any membranous material present. The distribution profile of the RNA in a second (='heavy') phytochrome fraction does not correlate with that of the pigment. This suggests that the phytochrome in this fraction is not bound to RNP. The RNA is of ribosomal origin but much less degraded than that of the 31S RNP and is resistant to RNase digestion. Phospholipase C releases > 80% of the [^<14>C]-choline from the 'heavy' faction without freeing phytochrome. This indicates that the pigment does not bind to the polar head groups of the membrane phospholipids present. Low concentrations of deoxycholate dissociate phytochrome from this fraction without releasing substantial quantities of integral membrane proteins or phospholipids. Some RNP is dislodged by the surfactant but the phytochrome and RNP are not released as a complex. The data suggest that the pigment in the 'heavy' fraction may be loosely bound to a protein constituent rather than to RNP or polar phospholipids.
- 日本植物生理学会の論文
著者
-
Gressel J.
Research School Of Biological Sciences Australian National University
-
Quail P.H.
Research School of Biological Sciences, Australian National University
-
Quail P.h.
Research School Of Biological Sciences Australian National University