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  • Cross-pathway control gene  (1)
  • Induction  (1)
  • Life and Medical Sciences  (1)
  • 1
    ISSN: 1617-4623
    Keywords: Laccase gene ; Transcriptional activation ; Cycloheximide ; Cross-pathway control gene ; Neurospora crassa
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Expression of the laccase gene (lacc) of Neurospora crassa is transcriptionally inducible by the protein synthesis inhibitor cycloheximide. A lni-1 mutation, conferring the laccase non-inducible phenotype, was found to be a cpc-1 allele. Northern blots probed with plasmid pLAI, which carries the lacc gene revealed that the cpc-1 mutation abolishes the induced transcription of the lacc gene, indicating requirement of the cpc-1 gene for transcriptional activation of the lacc gene. In Northern blots probed with plasmid pABI, which bears arg-2 a gene whose transcription is under the control of CPC1, the level of the arg-2 transcript was shown to increase several-fold in wild-type mycelia but remained low in cpc-1 mycelia, after treatment with cycloheximide. This suggests that inhibition of protein synthesis with cycloheximide, as well as amino acid limitation, elicits the CPC1-mediated cross-pathway control. Characterization of the lacc upstream region using a series of 5′-deletion plasmids led to the identification of a 170 bp DNA region required for the induced lacc expression. Sequence analysis of this DNA region demonstrated that it includes a 9 by sequence with dyad symmetry, ATGAATCAT which differs only by a central base pair from ATGA(C/G)TCAT the recognition sequence characteristic of CPC1 and GCN4 binding sites. Possible mechanisms by which CPC1 mediates transcriptional activation of the lacc gene are discussed.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1617-4623
    Keywords: Laccase ; Induction ; Cycloheximide ; Transcriptional regulation ; Neurospora crassa
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A protein synthesis inhibitor, cycloheximide, induces excretion of laccase in Neurospora crassa. The lah-1 mutation results in excretion of a large amount of laccase even in the absence of cycloheximide. Ten mutations were induced that suppress derepressed excretion of laccase in the lah-1 mutant. Of these, seven second-site mutations were found to confer a laccase-noninducible phenotype, and were classified into two different complementation groups. Four mutations define a locus designated lni-1, found to be closely linked to ylo-1 on linkage group VI. The other three mutations were mapped to second locus, designated lni-2, that lies between nic-3 and thi-3on linkage group VII. The lni-2 locus was shown to encode laccase by RFLP mapping of the DNA fragment encoding laccase and by transformation of the lni-2 mutant with plasmid pBLI carrying the laccase gene (the locus encoding laccase is hereafter described as lacc). All lacc mutants examined (whether mutagen-induced or inactivated by repeat-induced point mutation) appeared to exhibit no phenotypic deficiency during both asexual and sexual cycles, suggesting that the laccase gene is dispensable in N. crassa. Northern analysis of total cellular RNA from the four lni-1 mutants demonstrated that the lni-1 mutations abolish increased transcription of the laccase gene under inducing conditions. Consequently, the lni-1 locus is inferred to encode a trans-acting positive regulator required for transcriptional activation of the laccase gene in response to cycloheximide. Possible functions of the lah-1 gene are also described.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 145 (1990), S. 428-433 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Transformed Fisher rat fibroblast cell lines by Abelson murine leukemia virus frequently revert to the normal phenotype in usual culture conditions. Molecular Biological analysis of thre revertant clones isolated from the transformants showed that their morphological reversions were due to inactivation of the v-abl oncogene at multiple steps including transcription, translation or v-abl protein kinase activity itself without any change in structural gene expression of helper virus. These findings suggest the existence of a specific mechanism(s) for elimination of the v-abl oncogene by segregation, mutation, or gene rearrangement in these cells.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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