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벼 배유세포에서 (胚乳細胞) 분리된 미크로좀 내로의 저장 (貯藏) 단백질 이동
김우택,Xingxiang Li,Thomas W . Okita (Woo Taek Kim) 한국식물학회 1994 Journal of Plant Biology Vol.37 No.3
Developing rice endosperm cells display two morphologically distinct rough endoplasmic reticulum (ER) membranes, the cisternae ER (C-ER) and the protein body ER (PB-ER), the latter delimiting the prolamine protein bodies. We (Li et al., 1993) have recently shown that the storage protein mRNAs are not randomly distributed on these ER types; the C-ER is enriched for glutelin mRNAs, whereas the PB-ER harbors predominantly prolamine transcripts. To address whether these ER types have different capacities to translate these mRNAs and translocate their proteins into the lumen, a microsomal fraction enriched in C-ER vesicles was prepared from developing rice seeds When present in an in vitro translation system, the microsomes were able to proteolytically remove the signal peptide and internalize both preproglutelin and preprolamine within the microsomal vesicles. Of the two species, preprolamine was more effectively translocated and processed. These results suggest that the C-ER has the capacity to recognize and bind both storage protein mRNAs during protein synthesis. Moreover, efficient translocation and processing of glutelin requires additional factors that are deficient or absent in the in vitro system.