An oleosin-fusion protein driven by the CaMV35S promoter is accumulated in Arabidopsis (Brassicaceae) seeds and correctly targeted to oil bodies.
نویسندگان
چکیده
Oleosin-fusion technology is used to express desired proteins. It was developed based on the properties of oleosin; the heterologous protein gene is fused to the oleosin gene and the fusion gene is driven by a seed-specific promoter. We replaced the seed specific promoter with the CaMV35S promoter to dive a gfp-oleosin fusion gene in transformed Arabidopsis. The heterologous oleosin-fusion protein was mainly accumulated in the transgenic Arabidopsis seeds and correctly targeted to oil bodies. This provides an alternate choice of promoter in oleosin-fusion technology.
منابع مشابه
Oil-body-membrane proteins and their physiological functions in plants.
Oilseeds accumulate a large amount of storage lipids, which are used as sources of carbon and energy for seed germination and seedling growth. The storage lipids are accumulated in oil bodies during seed maturation. Oil bodies in seeds are surrounded with three oil-body-membrane protein families, oleosins, caleosins and steroleosins. These proteins are plant-specific and much abundant in seeds....
متن کاملProduction of Biologically Active Cecropin A Peptide in Rice Seed Oil Bodies
Cecropin A is a natural antimicrobial peptide that exhibits fast and potent activity against a broad spectrum of pathogens and neoplastic cells, and that has important biotechnological applications. However, cecropin A exploitation, as for other antimicrobial peptides, is limited by their production and purification costs. Here, we report the efficient production of this bioactive peptide in ri...
متن کاملRole of the proline knot motif in oleosin endoplasmic reticulum topology and oil body targeting.
An Arabidopsis oleosin was used as a model to study oleosin topology and targeting to oil bodies. Oleosin mRNA was in vitro translated with canine microsomes in a range of truncated forms. This allowed proteinase K mapping of the membrane topology. Oleosin maintains a conformation with a membrane-integrated hydrophobic domain flanked by N- and C-terminal domains located on the outer microsome s...
متن کاملStructural requirements of oleosin domains for subcellular targeting to the oil body.
We have investigated the protein domains responsible for the correct subcellular targeting of plant seed oleosins. We have attempted to study this targeting in vivo using "tagged" oleosins in transgenic plants. Different constructs were prepared lacking gene sequences encoding one of three structural domains of natural oleosins. Each was fused in frame to the Escherichia coli uid A gene encodin...
متن کاملGene family of oleosin isoforms and their structural stabilization in sesame seed oil bodies.
Oleosins are structural proteins sheltering the oil bodies of plant seeds. Two isoform classes termed H- and L-oleosin are present in diverse angiosperms. Two H-oleosins and one L-oleosin were identified in sesame oil bodies from the protein sequences deduced from their corresponding cDNA clones. Sequence analysis showed that the main difference between the H- and L-isoforms is an insertion of ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Genetics and molecular research : GMR
دوره 11 3 شماره
صفحات -
تاریخ انتشار 2012