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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Four different types of crosses have been used to establish the order of the four genes in the qa gene cluster of Neurospora crassa, which encode the following proteins involved in the inducible catabolism of quinic acid: a regulatory (activator) protein (qa-1), catabolic dehydroquinase (qa-2), quinate dehydrogenase (qa-3), and dehydroshikimate dehydrase (qa-4). The four crosses involved (1) the ordering of the four qa genes relative to the closely-linked me-7 locus; (2) the ordering of the three other qa genes relative to a qa-1S mutant; (3) the use of a three factor cross--qa-3 X qa-4 qa-2 and (4) the use of four factor crosses--qa-1S X qa-3 qa-4 qa-2. The results of all four types of crosses agree in establishing an apparently definitive proximal to distal order, within the right arm of linkage group VII, i.e., qa-1 qa-3 qa-4 qa-2 me-7. The significance of a definitive establishment of the gene order within the qa cluster for an understanding of the organization and mechanism of genetic regulation in this cluster is discussed.
Mol Gen Genet 1976 Aug 10
PMID:Gene order in the qa gene cluster of Neurospora crassa. 13 53

Mutants altered in carbon catabolite regulation have been isolated by selecting for mutants of the areA217 strain capable of using acetamide as the sole nitrogen source in the presence of sucrose. In addition to creA mutants described previously be Arst and Cove, strains with mutations in two new genes, creB and cre C, have been found. The creB and creC mutants grow poorly on some sole carbon sources and have low levels of some enzymes of carbon catabolism e.g. beta-galactosidase and D-quinate dehydrogenase. The creB and creC mutants are hypersensitive to fluoroacetate, fluoroacetamide and allyl alcohol in the presence of glucose or sucrose but not glycerol; and the enzymes, acetamidase and alcohol dehydrogenase, are less sensitive to carbon catabolite repression than the wild-type strain. Extracellular protease and alpha-glucosidase enzyme activities are elevated in creB and creC mutants, while L-proline and L-glutamate uptake capacities are lower in both the presence and absence of glucose. Interactions between creA, B and C mutations have been investigated in double mutants, and the dominance properties of creB and creC mutants determined. The results indicate that the creB and creC genes may have a regulatory role in the control of carbon catabolism.
Mol Gen Genet 1977 Jan 18
PMID:Pleiotropic mutants of Aspergillus nidulans altered in carbon metabolism. 32 Apr 55

A functional analysis of the Aspergillus nidulans 3-phosphoglycerate kinase pgk promoter was undertaken using gene fusions to the lacZ gene of Escherichia coli, and introducing these into a beta-galactosidase-deficient strain of A. nidulans. Expression of a particular gene fusion in transformed strains depends upon the site of integration of the vector into the genome, and when specifically targeted to the catabolic quinate dehydrogenase qutE (selective marker) locus is directly proportional to its copy number. The analysis of transformed strains with single copies of pgk promoter deletion--lacZ fusions at the qutE locus identified three constitutive, positively acting sequence elements in the pgk gene. Sequence located between -161 and -120 nucleotides relative to the transcript start site +1, and including an element with a seven-out-of-eight nucleotide match (AAGCAAAT; -131 to -124) to the consensus eukaryotic octamer sequence ATGCAAAT, is essential for expression, and deletion of the complete 41-nucleotide sequence abolishes transcription. Sequence encompassing codons 14 to 183 and including the two introns of pgk contributes approximately one-third of the total activity, and far upstream sequence 5' to position -638 contributes approximately a further one-third total activity. In addition, sequence located -638 to -488 nucleotides, which includes an apparent consensus feature of A. nidulans glycolytic genes, affects carbon source-dependent regulation of expression. This region is required for an approximately 50% increase in pgk expression when A. nidulans is grown on gluconeogenic compared with glycolytic carbon sources.
Mol Gen Genet 1992 May
PMID:Functional analysis of the expression of the 3'-phosphoglycerate kinase pgk gene in Aspergillus nidulans. 160 65

The functional integrity of the QUTB gene (encoding quinate dehydrogenase) has been confirmed by transformation of a qutB mutant strain. The DNA sequence of the contiguous genes QUTD (quinate permease), QUTB and QUTG (function unknown) has been determined and analysed, together with that of QUTE (catabolic 3-dehydroquinase). The QUTB sequence shows significant homology with the shikimate dehydrogenase function of the complex AROM locus of Aspergillus nidulans, and with the QA-3 quinate dehydrogenase and QA-1S (repressor) genes of Neurospora crassa. The QUTD gene shows strong homology with the N. crassa QA-Y gene and QUTG with the QA-X gene. QUTD, QUTB, and QUTG, QUTE form two pairs of divergently transcribed genes, and conserved sequence motifs identified in the two common 5' non-coding regions show significant homology with UASGAL and UASQA sequences of the Saccharomyces cerevisiae and N. crassa Gal and QA systems. In addition, conserved 5' sequences homologous to the mammalian CAAT box are noted and a previously unreported conserved 22 nucleotide motif is presented.
Mol Gen Genet 1988 Oct
PMID:Molecular organisation of the quinic acid utilization (QUT) gene cluster in Aspergillus nidulans. 297 80

An in vitro protein-synthesizing system (rabbit reticulocyte) was programmed with total polyadenylated messenger ribonucleic acid from wild type and various mutants in the qa gene cluster of Neurospora crassa. The products of two of the qa genes, quinate dehydrogenase (qa-3+) and dehydroshikimate dehydratase (qa-4+), were identified by specific immunoprecipitation and sodium dodecyl sulfate-slab gel electrophoresis. The results indicated that for both genes induction of a specific enzyme activity by quinic acid depends on the de novo synthesis of a specific polypeptide and on the de novo appearance of specific messenger ribonucleic acid detectable by the in vitro translation assay. Furthermore, the results indicated that the appearance of this messenger ribonucleic acid is under the control of the qa-1 gene. The simplest interpretation of these results appears to be that induction of enzyme activity in the qa system is mediated by events at the transcriptional level.
Mol Cell Biol 1981 Sep
PMID:Genetic regulation of the qa gene cluster of Neurospora crassa: induction of qa messenger ribonucleic acid and dependency on qa-1 function. 927 95