Chemistry: molecular biology and microbiology – Plant cell or cell line – per se ; composition thereof;... – Plant cell or cell line – per se – is pest or herbicide...
Patent
1994-11-25
1999-03-30
Benzion, Gary
Chemistry: molecular biology and microbiology
Plant cell or cell line, per se ; composition thereof;...
Plant cell or cell line, per se, is pest or herbicide...
435410, 435419, 4351723, 4351721, 800205, 536 231, 536 236, 935 10, 935 67, 935 69, 935 72, 935 76, C12N 1500, C12N 1509, C12N 1505, A01H 106
Patent
active
058888187
DESCRIPTION:
BRIEF SUMMARY
This invention relates to modified tubulins, DNA sequences encoding such tubulins and organisms transformed with such DNA.
Almost all eukaryotic cells contain microtubules which comprise a major component of the network of proteinaceous filaments known as the cytoskeleton. Microtubules thereby participate in the control of cell shape and intracellular transport. They are also the principal constituent of mitotic and meiotic spindles, cilia and flagella. In plants, microtubules have additional specialized roles in cell division and cell expansion during development.
In terms of their composition, microtubules are proteinaceous hollow rods with a diameter of approximately 24 nm and highly variable length. They are assembled from heterodimer subunits of an .alpha.-tubulin and a .beta.-tubulin polypeptide, each with a molecular weight of approximately 50,000. Both polypeptides are highly flexible globular proteins (approximately 445 amino acids), each with a predicted 25% .alpha. helical and 40% .beta.-pleated sheet content. In addition to the two major forms (.alpha.-and .beta.-tubulin), there is a rare .gamma.-tubulin form which does not appear to participate directly in the formation of microtubule structure, but rather it may function in the initiation of microtubule structure.
In all organisms, the multiple .alpha.- and .beta.-tubulin polypeptides are encoded by corresponding families of .alpha.- and .beta.-tubulin genes, which are located in the nuclear genome. Many such genes (or corresponding cDNAs) have been isolated and sequenced. For example, maize has approximately 6 .alpha.-tubulin genes and approximately 8 .beta.-tubulin genes dispersed over the genome (Villemur et al, 1992, 34th Maize Genetics Symposium). Some of the .alpha.-tubulin genes from maize have been cloned and sequenced (Montoliu et al, 1989, Plant Mol Biol, 14, 1-15; Montoliu et al, 1990, Gene, 94, 201-207; Villemur et al, 1992, J Mol Biol, 227:81-96), as have some of the .beta.-tubulin genes (Hussey et al, 1990, Plant Mol Biol, 15, 957-972). Comparison of amino acid sequences of the three documented maize .alpha.-tubulins indicates they have 93% homology. Maize .beta.-tubulins exhibit 38% identity with these .alpha.-tubulins. In segments of divergence between the .alpha.- and .beta.-tubulin amino acid sequences, homology ranges from 13% to 17%. Homology between the three .alpha.-tubulin amino acid sequences within these same .alpha.-/.beta.-divergence regions ranges from 77% to 96%.
Sequence information on the various tubulin forms shows that throughout evolution the protein domains involved in polymerization have been highly conserved, and interspecies amino acid sequence homology is generally high. For example, the four .beta.-tubulin isotypes in human are identical with their counterparts in mouse. There is 82-90% homology between mammalian neuronal or constitutively expressed tubulins and algal, protozoan and slime mould tubulins. Considering plant sequences in more detail, there are long stretches in which the amino acid sequence of all the .alpha.- and .beta.-tubulins are identical (Silflow et al, 1987, Developmental Genetics, 8, 435-460). For example, the 35 amino acids in positions 401-435 are identical in all plant .alpha.-tubulins, as are the 41 amino acids in the region between positions 240 and 281 in the plant .beta.-tubulins. Conservation of amino acid residues is approximately 40% between the .alpha.- and .beta.-tubulin families, and 85-90% within each of the .alpha.- and .beta.-tubulin families. It should be noted that in general, most .alpha.-tubulins are 1 to 5 residues larger that the .beta.-tubulins.
The economic interest of tubulins lies in the effect of certain agents which interfere with tubulin structure and/or function. Such agents (including non-chemical stresses) are hereinafter referred to as "anti-tubulin agents" as they share a similar type of mode of action. Extreme conditions are known to destabilize the tubulins and/or microtubules. Such conditions include cold, pressure and certain chemicals. For exa
REFERENCES:
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Cronin Kathryn Elizabeth
Ellis, deceased John Raymond
Hussey Patrick Joseph
Ray John Anthony
Waldin Teresa Ruth
Benzion Gary
Shaw Melissa A.
Zeneca Limited
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