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201.
Iñaki Alvarez M. Isabel Geli Eulogio Pimentel Dolors Ludevid Margarita Torrent 《Planta》1998,205(3):420-427
We have previously shown that the maize (Zea mays L.) storage prolamine γ-zein, accumulates in endoplasmic reticulum-derived protein bodies in transgenic plants of Arabidopsis thaliana (L.) ecotype R+P. The retention of γ-zein in the endoplasmic reticulum was found to be mediated by structural features contained
in the polypeptide, an N-terminal proline-rich and a C-terminal cysteine-rich domain which were necessary for the correct
retention and assembly of γ-zein within protein bodies (M.I. Geli et al., 1994, Plant Cell 6: 1911–1922). In the present work
we incorporated in the γ-zein gene lysine-rich coding sequences which were positioned after the N-terminal proline-rich domain
and at five amino-acid residues from the C-terminus. The targeting of lysine-rich γ-zeins was analyzed by expression of chimeric
genes regulated by the cauliflower mosaic virus (CaMV) 35S promoter in transgenic Arabidopsis plants. The lysine-rich γ-zeins were detected by immunoblotting and we found that these proteins were modified post-translationally
to reach their mature form. Subcellular fractionation and immunocytochemical studies demonstrated that glycosylated lysine-rich
γ-zeins were secreted to the cell wall of transgenic Arabidopsis leaf cells.
Received: 9 May 1997 / Accepted: 31 October 1997 相似文献
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Validating viral quasispecies with digital organisms: a re-examination of the critical mutation rate
Background
In this report we re-examine some recent experiments with digital organisms to test some predictions of quasispecies theory. These experiments revealed that under high mutation rates populations of less fit organisms previously adapted to such high mutation rates were able to outcompete organisms with higher average fitness but adapted to low mutation rates. 相似文献205.