2 edition of Nitrate and cytochrome-c reductases from wild-type and mutant strains of Aspergillus nidulans. found in the catalog.
Nitrate and cytochrome-c reductases from wild-type and mutant strains of Aspergillus nidulans.
Donald William Macdonald
Thesis (Ph.D.) - University of East Anglia, School of Biological Sciences, 1969.
Analysis of wild-type and mutant plant nitrate reductase expressed in the methylotrophic yeast Pichia pastoris. W Su, J A Mertens, K Kanamaru, W H Campbell, and N M Crawford Department of Biology, University of California, San Diego, La Jolla , USA. In fungi, transcriptional activation of genes involved in NO 3-assimilation requires the presence of an inducer (nitrate or nitrite) and low intracellular concentrations of the pathway products ammonium or glutamine. In Aspergillus nidulans, the two transcription factors NirA and AreA act synergistically to mediate nitrate/nitrite induction and nitrogen metabolite derepression, respectively.
Filamentous Fungal Strains—Aspergillus fumigatus strains used in this study were wild-type, cnx1 and cnx3 mutants, Aspergillus niger wild-type and niaD, and Aspergillus oryzae wild-type and niaD (all this study), and N. crassa wild-type, nit-3 (RIP), and nit (RIP). 1 Mutant nit-3 (RIP) was found to lack nitrate reductase activity and. Abstract. Mutants of Aspergillus nidulans resistant to methylammonium toxicity are simultaneously derepressed in the presence of ammonium for apparently all ammonium-repressible activities. Enzyme assays directly demonstrate derepression of nitrate, nitrite, and hydroxylamine reductases, xanthine dehydrogenase, urate oxidase, and allantoinase, whereas in vivo tests show that ammonium and.
Both periplasmic (Nap) and respiratory nitrate reductase (Nar) participate in nitrate respiration while a cytochrome c nitrite reductase is used for nitrite reduction . Moreover, E. coli can. Prokaryotic nitrate reductases have two major types, transmembrane nitrate reductases and periplasmic nitrate reductases. The transmembrane nitrate reductase (NAR) does proton translocation and can contribute to the generation of ATP by the proton motive force.
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Summary. The sedimentation coefficients of the NADPH: cytochrome-c oxidoreductase enzymes from wild-type and mutant strains of Aspergillus nidulans have been estimated by sucrose density gradient the wild-type, two species of cytochrome-c reductase were found, with sedimentation coefficients of s and s s species did not appear to be Cited by: 1.
Mol Gen Genet. Feb 6;(3) Cytochrome-c reductases from wild-type and mutant strains of Aspergillus nidulans.
MacDonald DW, Cove DJ, Coddington by: Summary. Six mutant strains (, and ) affected in their nitrate assimilation capability and their corresponding parental wild-type strains (c and 21gr) from Chlamydomonas reinhardii have been studied on different nitrogen sources with respect to NAD(P)H-nitrate reductase and its associated activities (NAD(P)H-cytochrome c reductase and reduced benzyl viologen Cited by: Summary.
Ten nitrate reductase-deficient Hordeum vulgare mutants were characterized for NADH and FMNH 2 nitrate reductase (NR), cytochrome C reductase (CR) and nitrite reductase (NiR) activities. The mutants sort into four major groups.
Group I represented by mutants Az 12, Az 23, Az 29 and Az 30 have low Nr and Cr by: A purification procedure for nitrate reductase (NADPH: nitrate oxidoreductase, EC ) from Aspergillus nidulans, is described which achieves a fold rome c reductase (NADPH:cytochrome c oxidoreductase, EC ) activity is found to be associated with the nitrate reductase activity throughout the purification, the ratio of the two activities remaining approximately Cited by: On a secondary screen, eleven clones were found to hybridize TABLE I Cytochrome c reductase activities of ChR resistance mutants Strain ~ Cytochrome c reductase activityb CSG27 CSG62 57 wt a Mutant isolation is described in Fig.
b NADPH cytochrome c reductase assays were performed in triplicate using a modification of published. No NADPH-nitrate reductase activity was found in extracts prepared by co-homogenizing mycelia from all five A. nidulans cnx strains.
Wild-type A. nidulans NADPH-nitrate reductase acid dissociated by adjustment to pH – and re-adjusted to pH 7 could itself re-assemble to form active nitrate reductase and thus was not a sueful source of. () have studied the sedimentation properties of NADPH-dependent cytochrome c reductase in wild type and mutant Aspergillus nidulans.
They find a pattern almost identical to that described in Neurospora. Both contain a S species which is not inducible by nitrate and probably unrelated to nitrate reductase. MacDonald DW, Cove DJ, Coddington A. Cytochrome-c reductases from wild-type and mutant strains of Aspergillus nidulans.
Mol Gen Genet. Feb 6; (3)– Moureaux T, Leydecker MT, Meyer C. Purification of nitrate reductase from Nicotiana plumbaginifolia by affinity chromatography using 5'AMP-sepharose and monoclonal antibodies. In vitro restoration of nitrate reductase: investigation of Aspergillus nidulans and Neurospora crassa nitrate reductase mutants.
Ketchum PA, Downey RJ. Extracts of Aspergillus nidulans wild type (bi-1) and the nitrate reductase mutant niaD were active in the in vitro restoration of NADPH-dependent nitrate reductase when mixed with extracts.
Cytochrome c reductases from wild-type and mutant strains of Aspergillus nidulans. Mol. Gen. Genet. D.J. CoveKinetic studies of the induction of nitrate reductase and cytochrome c reductase in the fungus Aspergillus nidulans.
Biochem. J, (), pp. Google Scholar. Nitrate induces cytochrome-c reductase activity in the mutant but to a lower level than in the wildtype.
and mutant strains of Aspergillus nidulans. from wild-type and mutant strains of. nidulans wild‐type strain (light grey bars) and a ΔfhbA ΔfhbB mutant (dark grey bars) were grown vegetatively in ammonium liquid medium for 18 h (VEG) and then transferred to solid media containing different nitrogen sources to induce development: ammonium tartrate as control nitrogen source (A), sodium nitrate (B) and sodium nitrate.
Two independent transformants, for TniaD and each site-directed mutant, derived from replacement integration plus the wild-type C5 and niaD78 strains, were grown under inducing (10 mM urea + 20 mM NO 3) and noninducing (10 mM urea) conditions and assayed for their nitrate reductase and nitrite reductase activities using crude mycelial extracts.
Chlamydomonas reinhardii wild strain c as well as the mutant strainwhich lacks NAD(P)H-nitrate reductase (EC ) activity and molybdenum-containing cofactor, exhibit and ammonia-repressible NAD(P)H-cytochrome c reductase activity of identical molecular size, 44 This diaphorase activity, which in both strains produces a fast-moving band on electrophoresis, has been.
In vitro restoration of Neurospora assimilatory nitrate reductase from protein subunits of a Neurospora mutant and the xanthine-oxidizing or aldehyde oxidase systems of higher animals.
Cytochrome-c reductases from wild-type and mutant strains of Aspergillus nidulans. MacDonald DW, Cove DJ, Coddington A. Cytochrome-c reductases from wild-type and mutant strains of Aspergillus nidulans.
Mol Gen Genet. Feb 6; (3)– Nitrate uptake and nitrite excretion activity in wild-type (WT) and NiR mutant strains due to the HANT systems I and II.
Strains M1, M2, M3, and M4, and the wild-type c were grown in ammonium and then transferred to medium containing μ m nitrate at. A. nidulans wild‐type strain (light grey bars) and a Δfhb A Δfhb B mutant (dark grey bars) were grown vegetatively in ammonium liquid medium for 18 h (VEG) and then transferred to solid media containing different nitrogen sources to induce development: ammonium tartrate as control nitrogen source (A), sodium nitrate (B) and sodium nitrate.
mixtures of induced nit-i with either uninduced nit-2 or wild type (Figs. 2A, B) was essentially the same as that of the wild-type enzyme (Fig. 2C). The single peak of NADPH-nitrate reductase activity (S20, = S) included the FADH2-and MVH-nitrate reductases and the inducible NADPH-cytochrome c reductase activity characteristically associated.
(A) A. nidulans wild-type, areA Δ, and areA strains were grown at 37°C for 2 days on ANM solid media containing 1% glucose and ammonium (NH 4), glutamine (Gln), glutamate (Glu), alanine (Ala), nitrate (NO 3), proline (Pro), γ-amino butyric acid (GABA), arginine (Arg), uric acid (UA), or histidine (His) at a final concentration of 10 mM as.A.
nidulans wild-type, Δ niaD and niiA4 strains were grown on solid media containing the indicated nitrogen sources at 10 mM (ammonium or nitrate) or 3 mM (proline) at 37°C for 18 h.Narendja F, Goller SP, Wolschek M, Strauss J.
Nitrate and the GATA factor AreA are necessary for in vivo binding of NirA, the pathway-specific transcriptional activator of Aspergillus nidulans.
Mol. Microbiol. ().