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Molecular organisation of the quinic acid utilization (QUT) gene cluster in Aspergillus nidulans
Authors:Alastair R Hawkins  Heather K Lamb  Melanie Smith  John W Keyte and Clive F Roberts
Institution:(1) Department of Genetics, University of Newcastle upon Tyne, NE2 4HH Newcastle upon Tyne, UK;(2) Department of Biochemistry, University of Leicester, LE1 7RH Leicester, UK;(3) Department of Genetics, University of Leicester, LE1 7RH Leicester, UK
Abstract:Summary 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 5prime non-coding regions show significant homology with UAS GAL and UAS QA sequences of the Saccharomyces cerevisiae and N. crassa Gal and QA systems. In addition, conserved 5prime sequences homologous to the mammalian CAAT box are noted and a previously unreported conserved 22 nucleotide motif is presented.
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