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  • 1
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 338 (1989), S. 662-664 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Three mutant mipA alleles were isolated as extragenic suppressors of benA33, a heat-sensitive (hs~) /3-tubulin mutation1'2'3. The ben A gene encodes the major /3-tubulin expressed in hyphae4 and this /3-tubulin is essential to mitosis and nuclear migration2'5. Although the mutant mipA alleles ...
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have isolated large numbers of conditionally lethal β-tubulin mutations to provide raw material for analyzing the structure and function of β tubulin and of microtubules. We have isolated such mutations as intragenic suppressors of benA33, a heat-sensitive (hs-) β-tubulin mutation of Aspergillus nidulans. Among over 2,600 revertants isolated, 126 were cold-sensitive (cs-). In 41 of 78 cs- revertants analyzed, cold sensitivity and reversion from hs- to hs+ were due to mutations linked to benA33. In three cases reversion was due to mutations closely linked to benA33 but cold sensitivity was due to a coincidental mutation unlinked to benA33. In the remaining 34 cases reversion was due to mutations unlinked to benA33. Thirty-three of the revertants in which cold sensitivity and reversion were linked to benA33 were sufficiently cold-sensitive to allow us to select for rare recombinants between benA33 and putative suppressors in a revertant x wild-type (wt) cross. We found only one recombinant among 1,000 or more viable progeny from crosses of each of these revertants with a wt strain. Reversion is thus due to a back mutation or very closely linked suppressor in each case. We have analyzed 17 of these 33 revertants with greater precision and have found that, in each case, reversion is due to a suppressor mutation that maps to the right of benA33. The recombination frequencies between benA33 and the suppressors are very low (less than 1.2×10-4) in all cases. Five of these 33 revertants have been examined microscopically and in each of them nuclear division and nuclear migration are inhibited at a restrictive temperature. We conclude that at least some and perhaps all of these revertants carry intragenic suppressors of benA33 that, in combination with benA33, cause cold sensitivity by inhibiting the functioning of microtubules at low temperatures. Of the 17 suppressors mapped, 11 map to two clusters. These clusters are likely to define regions particularly important to the functioning of the β-tubulin molecule.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 208 (1987), S. 135-144 
    ISSN: 1617-4623
    Keywords: Tubulin ; Microtubules ; Cytoskeleton ; Mitosis ; Motility
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have mapped 17 extragenic suppressors of benA 33, a heat-sensitive β-tubulin mutation of Aspergillus nidulans, to the tubA α tubulin locus. Fifteen of these tubA mutations cause cold sensitivity in a genetic background with benA 33 and appear to cause lethality in a background with the wild-type benA allele. We examined the microtubule-mediated processes, nuclear division and nuclear migration, in seven different cold-sensitive double mutants, each carrying benA 33 and a different cold-sensitive tubA allele. Nuclear division and migration were inhibited at a restrictive temperature in each case, suggesting that cold sensitivity is due to the inhibition of microtubule function at low temperatures. A single allele, tubA4, suppressed the heat sensitivity conferred by benA33 but did not confer cold sensitivity in a benA33 background, however in a wildtype benA background, tubA4 conferred supersensitivity to antimicrotubule agents and weak cold sensitivity. TubA4 did not suppress the heat sensitivity conferred by two other benA alleles. The cold sensitivity conferred by tubA4 was suppressed by the microtubule stabilizing agent deuterium oxide, and the suppression of heat sensitivity conferred by four other tubA mutations was reversed by deuterium oxide. These results suggest that these mutations may affect hydrophobic interactions between α-and β-tubulin.
    Type of Medium: Electronic Resource
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