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Plants and plants cells encoding wild type COP1 gene and coil domain thereof

A helical structure, plant cell technology, applied in angiosperms/flowering plants, botanical equipment and methods, biochemical equipment and methods, etc., can solve the impact, abnormal cotyledon growth and extension, seedling upward growth and unfavorable unearthed, etc. question

Inactive Publication Date: 2002-01-02
YALE UNIV
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, as described here and in McNellis et al. (1996), N-282-transformed plants have significant disadvantages in that they simultaneously exhibit abnormal cotyledon growth and extension when grown in the dark
As mentioned earlier, this will adversely affect the upward growth and emergence of seedlings

Method used

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  • Plants and plants cells encoding wild type COP1 gene and coil domain thereof
  • Plants and plants cells encoding wild type COP1 gene and coil domain thereof
  • Plants and plants cells encoding wild type COP1 gene and coil domain thereof

Examples

Experimental program
Comparison scheme
Effect test

example 1

[0141] For gel filtration chromatography, 8 day old light or dark grown seedlings are homogenized with 2X gel filtration buffer, centrifuged at 4°C for 5 minutes, the buffer contains 50mM Tris-HCl (pH7.5), 440mM NaCl, 2mM MgCl 2 , 2μM ZnSO 4 0.5mM PMSF. A 25ml Superdex-200 FPLC column (Pharmacia) and 1X gel filtration buffer were used to separate the completely soluble protein at a rate of 0.5ml / min. All processes are carried out at 4°C, and for dark samples, it is also under green safety light. After the dead volume (7.5ml), each successive 0.5ml fraction was collected, concentrated and subjected to 10% SDS-PAGE, followed by protein immunohybridization analysis. The molecular weight standards used to estimate the size of natural COP1 protein are as follows: blue dextran (invalid); thyroglobulin (669kDa); ferritin (440kDa); catalase (232kDa); aldolase (158kDa); BSA (67kDa); Ovalbumin (43kDa) and Ribonuclease A (13.7kDa) (Sigma). Example 1. COP1 forms dimers in vivo and in vitro

...

example 2

[0144] In order to further define the COP1 dimerization domain inside the COP1 N282 fragment, a series of deletion mutants of N282 were constructed and analyzed using the yeast two-hybrid system ( figure 1 C). The results indicate that the helical domain of COP1 is necessary for self-connection. Is also sufficient ( figure 1 C3, 1C4, 1C7 to 12C10). However, the lack of the helical domain on the N282 fragment can still produce weak and reproducible interactions, which are slightly stronger than the negative control (see figure 1 C1 to 1C4), indicating that there is residual COP1 self-association in other regions of the N-terminus. It seems that the ring finger domain is responsible for this residual activity, because this domain exhibits a weak interaction with itself ( figure 1 C5). The following results make it obvious that the ring finger in COP1 supports intramolecular linkage. In the complete C-terminal construct ( figure 1 C11 to 1C14), the deletion of the helical domain...

example 3

[0144] In order to further define the COP1 dimerization domain inside the COP1 N282 fragment, a series of deletion mutants of N282 were constructed and analyzed using the yeast two-hybrid system ( figure 1 C). The results indicate that the helical domain of COP1 is necessary for self-connection. Is also sufficient ( figure 1 C3, 1C4, 1C7 to 12C10). However, the lack of the helical domain on the N282 fragment can still produce weak and reproducible interactions, which are slightly stronger than the negative control (see figure 1 C1 to 1C4), indicating that there is residual COP1 self-association in other regions of the N-terminus. It seems that the ring finger domain is responsible for this residual activity, because this domain exhibits a weak interaction with itself ( figure 1 C5). The following results make it obvious that the ring finger in COP1 supports intramolecular linkage. In the complete C-terminal construct ( figure 1 C11 to 1C14), the deletion of the helical domain...

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Abstract

The present invention relates to a seedling which exhibits better germination characteristics when grown in the dark and whose growth is improved under conditions of low light levels. More specifically, the present invention relates to the preparation of plant cells and whole plants which contain a nucleotide sequence encoding a helical domain, together with a sequence encoding a wild-type COP1 gene. The plant of the present invention will form unopened and compact leaves when seedlings germinate in the dark, and the chlorosis phenomenon of seedlings grown under low light conditions after germination will be weakened. The present invention also relates to breeding methods that enable the transfer of these desirable traits into wild-type plants.

Description

[0001] Statement of Rights to Inventions under Federally Funded Research [0002] The present invention was partially completed by the government funded National Institutes of Health Grant No. GM47850. Invention field [0003] The present invention generally relates to the preparation of seedlings that exhibit better budding characteristics and improved growth under low light conditions. The present invention particularly relates to altering the genotype of plant cells to introduce a sequence encoding the helical domain of the COP1 protein. Background of the invention [0004] All publications and patent applications herein are incorporated by reference to the same degree, just as each individual publication or patent application specifically indicates that it is incorporated by reference. [0005] In the process of light morphogenesis, light provides an energy source for plants and ultimately to all living things. The light environment play...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): A01H5/00C07K14/415C12N5/10C12N15/09C12N15/29C12N15/82C12R1/91
CPCC07K14/415C12N15/8267C12N15/8261Y02A40/146
Inventor X·W·邓T·麦内利斯K·托里
Owner YALE UNIV
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