Synthesis of an unusual alpha-zein protein is correlated with the phenotypic effects of the floury2 mutation in maize.
Synthesis of an unusual alpha-zein protein is correlated with the phenotypic effects of the floury2 mutation in maize.
复制标题
一种不寻常的α-玉米醇溶蛋白的合成与玉米中floury2突变的表型效应相关。
DOI：
10.1007/bf00282216
复制
发表时间：
1994
期刊：
影响因子：
--
通讯作者：
Larkins,BA
中科院分区：
文献类型：
--
作者：
Lopes,MA;Coleman,CE;Kodrzycki,R;Lending,CR;Larkins,BA
The soft, starchy endosperm of the maize (Zea maysL)floury2mutant is associated with a reduction in zein mRNA and protein synthesis, unique protein body morphology, and enhanced levels of a 70 kDa protein, that has been shown to be the maize homolog of a chaperonin found in the endoplasmic reticulum. We found an unusual α-zein protein of 24 kDa to be consistently associated with the zein fraction fromfloury2mutants. Three additional α-zein proteins with molecular weights ranging from ca. 25 to 27 kDa are detected in the storage protein fraction of a high percentage offloury2kernels and a low percentage of normal kernels in a genetically segregating population. The four proteins can be distinguished from one another by immunostaining on Western blots. Synthesis of the 24 kDa protein is regulated byOpaque2, since the 24 kDa protein is lacking in the storage protein fraction ofopaque2/floury2double mutants. The synthesis of an abnormal a-zein protein infloury2could explain many features of the mutant, such as the abnormal protein body morphology, induction of the 70 kDa chaperonin, and hypostasis toopaque2 (o2). Although we cannot prove that the accumulation of this protein is responsible for thefloury2phenotype, we were able to detect a restriction fragment length polymorphism (RFLP) linked to thefloury2locus with a 22 kDa α-zein probe. We hypothesize that the unique characteristics of thefloury2mutant could be a response to the accumulation of a defective a-zein protein which impairs secretory protein synthesis.
