Transformation of Penicillium griseoroseum nitrate reductase mutant with the nia gene from Fusarium oxysporum

1998 ◽  
Vol 44 (5) ◽  
pp. 487-489 ◽  
Author(s):  
Marisa V de Queiroz ◽  
Andréa O Barros ◽  
Everaldo G de Barros ◽  
Walter V Guimarães ◽  
Elza F de Araújo
Keyword(s):  
Nitrate Reductase ◽  
Fusarium Oxysporum ◽  
Structural Gene ◽  
Dna Hybridization ◽  
Transformation System ◽  
Genetic Studies ◽  
Penicillium Griseoroseum ◽  
Heterologous Transformation ◽  
Tandem Arrays

A heterologous transformation system for Penicillium griseoroseum has been developed. This system is based on nia, the structural gene from Fusarium oxysporum encoding nitrate reductase. Penicillium griseoroseum niaD mutants have been selected from chlorate-resistant colonies. Among 24 chlorate-resistant colonies analyzed, 2 were confirmed to be niaD mutants. Transformation frequencies of 8 transformants/µg of DNA were obtained. DNA hybridization analyses of five transformants showed distinct integration patterns of the plasmid and in all of them the integration occurred at tandem arrays. The transformation system established in this work will be useful for genetic studies of the pectinolytic complex genes from P. griseoroseum.Key words: Penicillium griseoroseum, heterologous transformation, nitrate reductase.

scholarly journals Development of a transformation system for Penicillium brevicompactum based on the Fusarium oxysporum nitrate reductase gene

2005 ◽  
Vol 36 (2) ◽  
Author(s):  
Maurílio Antônio Varavallo ◽  
Marisa Vieira de Queiroz ◽  
Jorge Fernando Pereira ◽  
Ronney Adriano Ribeiro ◽  
Marcos Antônio Soares ◽  
...  
Keyword(s):  
Nitrate Reductase ◽  
Fusarium Oxysporum ◽  
Transformation System ◽  
Nitrate Reductase Gene ◽  
Reductase Gene ◽  
Penicillium Brevicompactum

Transformation of Penicillium griseoroseum nitrate reductase mutant with the nia gene from Fusarium oxysporum

1998 ◽  
Vol 44 (5) ◽  
pp. 487-489 ◽  
Author(s):  
Marisa V. de Queiroz ◽  
Andréa O. Barros ◽  
Everaldo G. de Barros ◽  
Walter V. Guimarães ◽  
Elza F. de Araújo
Keyword(s):  
Nitrate Reductase ◽  
Fusarium Oxysporum ◽  
Penicillium Griseoroseum ◽  
I Gene

scholarly journals Characterization, regulation, and phylogenetic analyses of thePenicillium griseoroseumnitrate reductase gene and its use as selection marker for homologous transformation

2004 ◽  
Vol 50 (11) ◽  
pp. 891-900 ◽  
Author(s):  
Jorge Fernando Pereira ◽  
Marisa Vieira de Queiroz ◽  
Francis Júlio Fagundes Lopes ◽  
Rodrigo Barros Rocha ◽  
Marie-Josée Daboussi ◽  
...  
Keyword(s):  
Nitrate Reductase ◽  
Nitrogen Metabolism ◽  
Phylogenetic Analyses ◽  
Regulatory Region ◽  
Selection Marker ◽  
Pcr Analysis ◽  
Transformation System ◽  
Homologous Transformation ◽  
Reductase Gene ◽  
Penicillium Griseoroseum

Penicillium griseoroseum has been studied because of its efficient pectinases production. In this work, the Penicillium griseoroseum nitrate reductase gene was characterized, transcriptionaly analyzed in different nitrogen sources, and used to create a phylogenetic tree and to develop a homologous transformation system. The regulatory region contained consensus signals involved in nitrogen metabolism and the structural region was possibly interrupted by 6 introns coding for a deduced protein with 864 amino acids. RT–PCR analysis revealed high amounts of niaD transcript in the presence of nitrate. Transcription was repressed by ammonium, urea, and glutamine showing an efficient turnover of the niaD mRNA. Phylogenetics analysis showed distinct groups clearly separated in accordance with the classical taxonomy. A mutant with a 122-bp deletion was used in homologous transformation experiments and showed a transformation frequency of 14 transformants/µg DNA. All analyzed transformants showed that both single- and double-crossover recombination occurred at the niaD locus. The establishment of this homologous transformation system is an essential step for the improvement of pectinase production in Penicillium griseoroseum.Key words: nitrate reductase, nitrogen metabolism, Penicillium griseoroseum, phylogenetic analysis, homologous transformation.

scholarly journals Establishment of a Tractable Genetic Transformation System in Veillonella spp.

2012 ◽  
Vol 78 (9) ◽  
pp. 3488-3491 ◽  
Author(s):  
Jinman Liu ◽  
Zhoujie Xie ◽  
Justin Merritt ◽  
Fengxia Qi
Keyword(s):  
Escherichia Coli ◽  
Genetic Transformation ◽  
Shuttle Vector ◽  
Transformation System ◽  
Genetic Studies ◽  
Content Type ◽  
Genetic Transformation System

ABSTRACTWe have constructed the firstEscherichia coli-Veillonellashuttle vector based on an endogenous plasmid (pVJL1) isolated from a clinicalVeillonellastrain. A highly transformableVeillonellastrain was also identified. Both the shuttle vector and the transformable strain should be valuable tools for futureVeillonellagenetic studies.

Identification of the Arabidopsis CHL3 Gene as the Nitrate Reductase Structural Gene NIA2

1991 ◽  
Vol 3 (5) ◽  
pp. 461 ◽  
Author(s):  
Jack Q. Wilkinson ◽  
Nigel M. Crawford
Keyword(s):  
Nitrate Reductase ◽  
Structural Gene

Distinction of cnxH cofactor gene-specified protomers with monoclonal antibodies to Aspergillus nitrate reductase

1988 ◽  
Vol 34 (1) ◽  
pp. 68-72 ◽  
Author(s):  
R. J. Downey ◽  
P. A. South
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Nitrate Reductase ◽  
Aspergillus Nidulans ◽  
Structural Gene ◽  
Molybdenum Cofactor ◽  
Native Enzyme ◽  
Wild Type ◽  
Dimeric Form

The nitrate reductase (NADPH) (EC 1.6.6.3) from Aspergillus nidulans is influenced directly by mutations in the structural gene (niaD) for the major subunit of the enzyme and indirectly by mutation in any of several molybdenum cofactor loci (cnx). The cnxE-14 and the cnxH-3 mutants have been noted to contain the enzyme in two distinct forms following induction with nitrate. With the cnxH-3 as a prototype cnxH mutant, 10 other cnxH were found to be devoid of the assembled (dimeric) form of the enzyme. Two monoclonal antibodies specific for the native enzyme of the wild type (biA-1) recognized an epitope on the enzyme from the cnxE-14 and cnxH-3 mutants that was common to both and another that was unique to the cnxH gene specified protomer. Another monoclonal antibody recognized an epitope that occurs only in the assembled dimeric form of the enzyme from the wild type or the cnxE-14 mutant. The experiments further substantiate the cnxH phenotype as one involving unassembled protomers of the nitrate reductase in Aspergillus.

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