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  • 1
    Electronic Resource
    Electronic Resource
    Analysis of actin and actin-related protein 3 (ARP3) gene expression following induction of hyphal tip formation and apolar growth in Neurospora (1998)
    Springer
    Molecular genetics and genomics 259 (1998), S. 601-609 
    Details
    ISSN: 1617-4623
    Keywords: Key wordsNeurospora crassa ; Actin ; Actin-related protein 3 (ARP3) ; cot-1 ; mcb
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The genes encoding actin and ARP3 in the filamentous fungus Neurospora crassa were cloned and sequenced. The actin structural gene is interrupted by four introns and encodes a polypeptide of 375 amino acids, which shows very high degree of identity with actin from other sources. N. crassa ARP3 is 439 amino acids in length and is 71% to 80% identical to ARP3s from five other organisms, while actin is 40% to 50% identical to these same ARP3s. Transcript levels for actin and ARP3 decrease upon induction of asexual development (i.e. conidiation) and subsequently increase slightly when conidia are being formed. A concentration of filamentous actin is typically seen at sites of growth in eukaryotic organisms and, using indirect immunofluorescence, we showed that filamentous actin is localized primarily to hyphal tips in N. crassa. To determine if the level of actin increases in response to an increase in the number of growth sites and in the area of the growing surface, we used the temperature-sensitive mutants cot-1 and mcb. Growth of the cot-1 and mcb mutants at restrictive temperature induces hyphal tip formation and a loss of growth polarity, respectively. Unexpectedly, almost no increase in actin levels is observed following a 〉20-fold increase in the number of hyphal tips or an increase in the area of the growing surface resulting from a loss of growth polarity. The results suggest that the level of actin monomers within N. crassa hyphae is sufficient to accommodate the need for additional actin patches and filaments that arises when the number of hyphal tips and the area of growing surface per unit length of hypha greatly exceeds that in wild-type.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050853
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  • 2
    Electronic Resource
    Electronic Resource
    A Neurospora crassa Arp1 mutation affecting cytoplasmic dynein and dynactin localization (2000)
    Springer
    Molecular genetics and genomics 264 (2000), S. 433-440 
    Details
    ISSN: 1617-4623
    Keywords: Cytoplasmic dynein Dynactin p150Glued Arp1 Microtubules
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. Of the actin-related proteins, Arp1 is the most similar to conventional actin, and functions solely as a component of the multisubunit complex dynactin. Dynactin has been identified as an activator of the microtubule-associated motor cytoplasmic dynein. The role of Arp1 within dynactin is two-fold: (1) it serves as a structural scaffold protein for other dynactin subunits; and (2) it has been proposed to link dynactin, and thereby dynein, with membranous cargo via interaction with spectrin. Using the filamentous fungus Neurospora crassa, we have identified genes encoding subunits of cytoplasmic dynein and dynactin. In this study, we describe a genetic screen for N. crassa Arp1 (ro-4) mutants that are defective for dynactin function. We report that the ro-4(E8) mutant is unusual in that it shows alterations in the localization of cytoplasmic dynein and dynactin and in microtubule organization. In the mutant, dynein/dynactin complexes co-localize with bundled microtubules at hyphal tips. Given that dynein transports membranous cargo from hyphal tips to distal regions, the cytoplasmic dynein and dynactin complexes that accumulate along microtubule tracts at hyphal tips in the ro-4(E8) mutant may have either reduced motor activity or be delayed for activation of motor activity following cargo binding.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380000304
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    Paper (German National Licenses)
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