Schaap PJ

References (6)

Title : Forward Genetics by Genome Sequencing Uncovers the Central Role of the Aspergillus niger goxB Locus in Hydrogen Peroxide Induced Glucose Oxidase Expression - Laothanachareon_2018_Front.Microbiol_9_2269
Author(s) : Laothanachareon T , Tamayo-Ramos JA , Nijsse B , Schaap PJ
Ref : Front Microbiol , 9 :2269 , 2018
Abstract : Aspergillus niger is an industrially important source for gluconic acid and glucose oxidase (GOx), a secreted commercially important flavoprotein which catalyses the oxidation of beta-D-glucose by molecular oxygen to D-glucolactone and hydrogen peroxide. Expression of goxC, the GOx encoding gene and the concomitant two step conversion of glucose to gluconic acid requires oxygen and the presence of significant amounts of glucose in the medium and is optimally induced at pH 5.5. The molecular mechanisms underlying regulation of goxC expression are, however, still enigmatic. Genetic studies aimed at understanding GOx induction have indicated the involvement of at least seven complementation groups, for none of which the molecular basis has been resolved. In this study, a mapping-by-sequencing forward genetics approach was used to uncover the molecular role of the goxB locus in goxC expression. Using the Illumina and PacBio sequencing platforms a hybrid high quality draft genome assembly of laboratory strain N402 was obtained and used as a reference for mapping of genomic reads obtained from the derivative NW103:goxB mutant strain. The goxB locus encodes a thioredoxin reductase. A deletion of the encoding gene in the N402 parent strain led to a high constitutive expression level of the GOx and the lactonase encoding genes required for the two-step conversion of glucose in gluconic acid and of the catR gene encoding catalase R. This high constitutive level of expression was observed to be irrespective of the carbon source and oxidative stress applied. A model clarifying the role of GoxB in the regulation of the expression of goxC involving hydrogen peroxide as second messenger is presented.
ESTHER : Laothanachareon_2018_Front.Microbiol_9_2269
PubMedSearch : Laothanachareon_2018_Front.Microbiol_9_2269
PubMedID: 30319579
Gene_locus related to this paper: aspna-g3y5a6

Title : Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015 versus enzyme-producing CBS 513.88 - Andersen_2011_Genome.Res_21_885
Author(s) : Andersen MR , Salazar MP , Schaap PJ , van de Vondervoort PJ , Culley D , Thykaer J , Frisvad JC , Nielsen KF , Albang R , Albermann K , Berka RM , Braus GH , Braus-Stromeyer SA , Corrochano LM , Dai Z , van Dijck PW , Hofmann G , Lasure LL , Magnuson JK , Menke H , Meijer M , Meijer SL , Nielsen JB , Nielsen ML , van Ooyen AJ , Pel HJ , Poulsen L , Samson RA , Stam H , Tsang A , van den Brink JM , Atkins A , Aerts A , Shapiro H , Pangilinan J , Salamov A , Lou Y , Lindquist E , Lucas S , Grimwood J , Grigoriev IV , Kubicek CP , Martinez D , van Peij NN , Roubos JA , Nielsen J , Baker SE
Ref : Genome Res , 21 :885 , 2011
Abstract : The filamentous fungus Aspergillus niger exhibits great diversity in its phenotype. It is found globally, both as marine and terrestrial strains, produces both organic acids and hydrolytic enzymes in high amounts, and some isolates exhibit pathogenicity. Although the genome of an industrial enzyme-producing A. niger strain (CBS 513.88) has already been sequenced, the versatility and diversity of this species compel additional exploration. We therefore undertook whole-genome sequencing of the acidogenic A. niger wild-type strain (ATCC 1015) and produced a genome sequence of very high quality. Only 15 gaps are present in the sequence, and half the telomeric regions have been elucidated. Moreover, sequence information from ATCC 1015 was used to improve the genome sequence of CBS 513.88. Chromosome-level comparisons uncovered several genome rearrangements, deletions, a clear case of strain-specific horizontal gene transfer, and identification of 0.8 Mb of novel sequence. Single nucleotide polymorphisms per kilobase (SNPs/kb) between the two strains were found to be exceptionally high (average: 7.8, maximum: 160 SNPs/kb). High variation within the species was confirmed with exo-metabolite profiling and phylogenetics. Detailed lists of alleles were generated, and genotypic differences were observed to accumulate in metabolic pathways essential to acid production and protein synthesis. A transcriptome analysis supported up-regulation of genes associated with biosynthesis of amino acids that are abundant in glucoamylase A, tRNA-synthases, and protein transporters in the protein producing CBS 513.88 strain. Our results and data sets from this integrative systems biology analysis resulted in a snapshot of fungal evolution and will support further optimization of cell factories based on filamentous fungi.
ESTHER : Andersen_2011_Genome.Res_21_885
PubMedSearch : Andersen_2011_Genome.Res_21_885
PubMedID: 21543515
Gene_locus related to this paper: aspna-g3y4g9 , aspna-g3yal2 , aspna-g3ycq2 , aspnc-a2qbh3 , aspnc-a2qe77 , aspnc-a2qf54 , aspnc-a2qfe9 , aspnc-a2qg33 , aspnc-a2qh76 , aspnc-a2qhe2 , aspnc-a2qi32 , aspnc-a2ql89 , aspnc-a2ql90 , aspnc-a2qla0 , aspnc-a2qmk5 , aspnc-a2qn56 , aspnc-a2qs22 , aspnc-a2qti9 , aspnc-a2qtz0 , aspnc-a2quc1 , aspnc-a2qx92 , aspnc-a2qyf0 , aspnc-a2qys7 , aspnc-a2qz72 , aspnc-a2qzn6 , aspnc-a2qzr0 , aspnc-a2qzx0 , aspnc-a2qzx4 , aspnc-a2r0p4 , aspnc-a2r1r5 , aspnc-a2r2i5 , aspnc-a2r5r4 , aspnc-a2r6h5 , aspnc-a2r8r3 , aspnc-a2r8z3 , aspnc-a2r273 , aspnc-a2r496 , aspnc-a2r502 , aspnc-a5abe5 , aspnc-a5abe8 , aspnc-a5abh9 , aspnc-a5abk1 , aspnc-axe1 , aspnc-cuti1 , aspnc-cuti2 , aspng-a2qs46 , aspng-a2qv27 , aspni-EstA , aspkw-g7y0v7 , aspnc-a2qt47 , aspnc-a2qt66 , aspna-g3xpq9 , aspnc-a2qqa1 , aspna-g3xsl3 , aspna-g3y5a6 , aspna-g3xpw9 , aspaw-a0a401kpx5 , aspnc-a2qw57 , aspaw-a0a401kcz4 , aspna-alba , aspna-azac

Title : 3DM: systematic analysis of heterogeneous superfamily data to discover protein functionalities - Kuipers_2010_Proteins_78_2101
Author(s) : Kuipers RK , Joosten HJ , van Berkel WJ , Leferink NG , Rooijen E , Ittmann E , van Zimmeren F , Jochens H , Bornscheuer U , Vriend G , dos Santos VA , Schaap PJ
Ref : Proteins , 78 :2101 , 2010
Abstract : Ten years of experience with molecular class-specific information systems (MCSIS) such as with the hand-curated G protein-coupled receptor database (GPCRDB) or the semiautomatically generated nuclear receptor database has made clear that a wide variety of questions can be answered when protein-related data from many different origins can be flexibly combined. MCSISes revolve around a multiple sequence alignment (MSA) that includes "all" available sequences from the entire superfamily, and it has been shown at many occasions that the quality of these alignments is the most crucial aspect of the MCSIS approach. We describe here a system called 3DM that can automatically build an entire MCSIS. 3DM bases the MSA on a multiple structure alignment, which implies that the availability of a large number of superfamily members with a known three-dimensional structure is a requirement for 3DM to succeed well. Thirteen MCSISes were constructed and placed on the Internet for examination. These systems have been instrumental in a large series of research projects related to enzyme activity or the understanding and engineering of specificity, protein stability engineering, DNA-diagnostics, drug design, and so forth.
ESTHER : Kuipers_2010_Proteins_78_2101
PubMedSearch : Kuipers_2010_Proteins_78_2101
PubMedID: 20455266

Title : Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88 - Pel_2007_Nat.Biotechnol_25_221
Author(s) : Pel HJ , de Winde JH , Archer DB , Dyer PS , Hofmann G , Schaap PJ , Turner G , de Vries RP , Albang R , Albermann K , Andersen MR , Bendtsen JD , Benen JA , van den Berg M , Breestraat S , Caddick MX , Contreras R , Cornell M , Coutinho PM , Danchin EG , Debets AJ , Dekker P , van Dijck PW , van Dijk A , Dijkhuizen L , Driessen AJ , d'Enfert C , Geysens S , Goosen C , Groot GS , de Groot PW , Guillemette T , Henrissat B , Herweijer M , van den Hombergh JP , van den Hondel CA , van der Heijden RT , van der Kaaij RM , Klis FM , Kools HJ , Kubicek CP , van Kuyk PA , Lauber J , Lu X , van der Maarel MJ , Meulenberg R , Menke H , Mortimer MA , Nielsen J , Oliver SG , Olsthoorn M , Pal K , van Peij NN , Ram AF , Rinas U , Roubos JA , Sagt CM , Schmoll M , Sun J , Ussery D , Varga J , Vervecken W , van de Vondervoort PJ , Wedler H , Wosten HA , Zeng AP , van Ooyen AJ , Visser J , Stam H
Ref : Nat Biotechnol , 25 :221 , 2007
Abstract : The filamentous fungus Aspergillus niger is widely exploited by the fermentation industry for the production of enzymes and organic acids, particularly citric acid. We sequenced the 33.9-megabase genome of A. niger CBS 513.88, the ancestor of currently used enzyme production strains. A high level of synteny was observed with other aspergilli sequenced. Strong function predictions were made for 6,506 of the 14,165 open reading frames identified. A detailed description of the components of the protein secretion pathway was made and striking differences in the hydrolytic enzyme spectra of aspergilli were observed. A reconstructed metabolic network comprising 1,069 unique reactions illustrates the versatile metabolism of A. niger. Noteworthy is the large number of major facilitator superfamily transporters and fungal zinc binuclear cluster transcription factors, and the presence of putative gene clusters for fumonisin and ochratoxin A synthesis.
ESTHER : Pel_2007_Nat.Biotechnol_25_221
PubMedSearch : Pel_2007_Nat.Biotechnol_25_221
PubMedID: 17259976
Gene_locus related to this paper: aspna-g3yal2 , aspnc-a2q8r7 , aspnc-a2q814 , aspnc-a2qb93 , aspnc-a2qbd3 , aspnc-a2qbh3 , aspnc-a2qbx7 , aspnc-a2qdj6 , aspnc-a2qe77 , aspnc-a2qf54 , aspnc-a2qfe9 , aspnc-a2qg33 , aspnc-a2qgj6 , aspnc-a2qgm6 , aspnc-a2qh52 , aspnc-a2qh76 , aspnc-a2qh85 , aspnc-a2qhe2 , aspnc-a2qi32 , aspnc-a2qib2 , aspnc-a2qk14 , aspnc-a2ql23 , aspnc-a2ql89 , aspnc-a2ql90 , aspnc-a2qla0 , aspnc-a2qlz0 , aspnc-a2qm14 , aspnc-a2qmk5 , aspnc-a2qms0 , aspnc-a2qn29 , aspnc-a2qn56 , aspnc-a2qn70 , aspnc-a2qnw9 , aspnc-a2qr21 , aspnc-a2qs22 , aspnc-a2qt50 , aspnc-a2qti9 , aspnc-a2qtz0 , aspnc-a2quc1 , aspnc-a2qw06 , aspnc-a2qwz6 , aspnc-a2qx92 , aspnc-a2qyf0 , aspnc-a2qys7 , aspnc-a2qz72 , aspnc-a2qzn6 , aspnc-a2qzr0 , aspnc-a2qzs1 , aspnc-a2qzx0 , aspnc-a2qzx4 , aspnc-a2r0p4 , aspnc-a2r0u0 , aspnc-a2r1p3 , aspnc-a2r1r5 , aspnc-a2r2i5 , aspnc-a2r2l0 , aspnc-a2r3s8 , aspnc-a2r4c0 , aspnc-a2r4j8 , aspnc-a2r5r4 , aspnc-a2r6g3 , aspnc-a2r6h5 , aspnc-a2r6h8 , aspnc-a2r7q1 , aspnc-a2r8r3 , aspnc-a2r8z3 , aspnc-a2r9y8 , aspnc-a2r032 , aspnc-a2r040 , aspnc-a2r273 , aspnc-a2r496 , aspnc-a2r502 , aspnc-a2ra07 , aspnc-a2rap4 , aspnc-a2raq2 , aspnc-a2rav1 , aspnc-a5aaf4 , aspnc-a5ab63 , aspnc-a5abc6 , aspnc-a5abe5 , aspnc-a5abe8 , aspnc-a5abf0 , aspnc-a5abh9 , aspnc-a5abk1 , aspnc-a5abt2 , aspnc-a5abz1 , aspnc-atg15 , aspnc-axe1 , aspnc-cuti1 , aspnc-cuti2 , aspnc-faec , aspng-a2q8w0 , aspng-a2qs46 , aspng-a2qst4 , aspng-a2qv27 , aspng-a2qzk9 , aspng-a2r0p8 , aspng-a2r225 , aspng-DAPB , aspng-DPP5 , aspng-faeb , aspni-APSC , aspni-EstA , aspni-FAEA , aspni-PAPA , aspkw-g7y0v7 , aspnc-a2qt47 , aspnc-a2qt66 , aspnc-a2r199 , aspnc-a2r871 , aspnc-a2qbp6 , aspnc-a2qqa1 , aspnc-a2qt70 , aspna-g3y5a6 , aspna-g3xpw9 , aspnc-a2qw57 , aspaw-a0a401kcz4 , aspna-alba , aspnc-kex1 , aspnc-cbpya , aspnc-a2qbg8

Title : Characterisation of Aspergillus niger prolyl aminopeptidase - Basten_2005_Mol.Genet.Genomics_272_673
Author(s) : Basten DE , Moers AP , Ooyen AJ , Schaap PJ
Ref : Mol Genet Genomics , 272 :673 , 2005
Abstract : We have cloned a gene (papA) that encodes a prolyl aminopeptidase from Aspergillus niger. Homologous genes are present in the genomes of the Eurotiales A. nidulans, A. fumigatus and Talaromyces emersonii, but the gene is not present in the genome of the yeast Saccharomyces cerevisiae. Cell extracts of strains overexpressing the gene under the control of its own promoter showed a fourfold to sixfold increase in prolyl aminopeptidase activity, but no change in phenylalanine or leucine aminopeptidase activity. The overexpressed enzyme was subsequently purified and characterised. The enzyme specifically removes N-terminal proline and hydroxyproline residues from peptides. It is the first enzyme of its kind from a eukaryotic organism that has been characterised.
ESTHER : Basten_2005_Mol.Genet.Genomics_272_673
PubMedSearch : Basten_2005_Mol.Genet.Genomics_272_673
PubMedID: 15654623
Gene_locus related to this paper: aspni-PAPA , emeni-q5bbi8

Title : Aminopeptidase C of Aspergillus niger is a novel phenylalanine aminopeptidase - Basten_2003_Appl.Environ.Microbiol_69_1246
Author(s) : Basten DE , Dekker PJ , Schaap PJ
Ref : Applied Environmental Microbiology , 69 :1246 , 2003
Abstract : A novel enzyme with a specific phenylalanine aminopeptidase activity (ApsC) from Aspergillus niger (CBS 120.49) has been characterized. The derived amino acid sequence is not similar to any previously characterized aminopeptidase sequence but does share similarity with some mammalian acyl-peptide hydrolase sequences. ApsC was found to be most active towards phenylalanine beta-naphthylamide (F-beta NA) and phenylalanine para-nitroanilide (F-pNA), but it also displayed activity towards other amino acids with aromatic side chains coupled to beta NA; other amino acids with non-aromatic side chains coupled to either pNA or beta NA were not hydrolyzed or were poorly hydrolyzed. ApsC was not able to hydrolyze N-acetylalanine-pNA, a substrate for acyl-peptide hydrolases.
ESTHER : Basten_2003_Appl.Environ.Microbiol_69_1246
PubMedSearch : Basten_2003_Appl.Environ.Microbiol_69_1246
PubMedID: 12571053
Gene_locus related to this paper: aspni-APSC