Un autoinductor de la biosíntesis de penicilina en Penicillium chrysogenum: caracterización molecular y estudio de la respuesta del proteoma a la adición de inductor = A penicillin biosynthesis self-inductor in Penicillium chrysogenum: Molecular characterization and study of the proteome response to the addition of the inductor

2010 ◽  
Author(s):  
Jorge Martín González
Keyword(s):  
Molecular Characterization ◽  
Penicillium Chrysogenum ◽  
Penicillin Biosynthesis

scholarly journals Localization of the pathway of the penicillin biosynthesis in Penicillium chrysogenum.

1991 ◽  
Vol 10 (2) ◽  
pp. 489-495 ◽  
Author(s):  
W. H. Müller ◽  
T. P. van der Krift ◽  
A. J. Krouwer ◽  
H. A. Wösten ◽  
L. H. van der Voort ◽  
...  
Keyword(s):  
Penicillium Chrysogenum ◽  
Penicillin Biosynthesis

scholarly journals Gene Targeting in Penicillium chrysogenum: Disruption of the lys2 Gene Leads to Penicillin Overproduction

1999 ◽  
Vol 181 (4) ◽  
pp. 1181-1188 ◽  
Author(s):  
Javier Casqueiro ◽  
Santiago Gutiérrez ◽  
Oscar Bañuelos ◽  
Maria Jose Hijarrubia ◽  
Juan Francisco Martín
Keyword(s):  
Penicillium Chrysogenum ◽  
Reductase Activity ◽  
Gene Replacement ◽  
Lysine Biosynthesis ◽  
Homologous Region ◽  
Crossing Over ◽  
Penicillin Biosynthesis ◽  
Single Crossing ◽  
Or Gene ◽  
Acid Precursor

ABSTRACT Two strategies have been used for targeted integration at thelys2 locus of Penicillium chrysogenum. In the first strategy the disruption of lys2 was obtained by a single crossing over between the endogenous lys2 and a fragment of the same gene located in an integrative plasmid.lys2-disrupted mutants were obtained with 1.6% efficiency when the lys2 homologous region was 4.9 kb, but no homologous integration was observed with constructions containing a shorter homologous region. Similarly,lys2-disrupted mutants were obtained by a double crossing over (gene replacement) with an efficiency of 0.14% by using two lys2 homologous regions of 4.3 and 3.0 kb flanking thepyrG marker. No homologous recombination was observed when the selectable marker was flanked by short lys2 homologous DNA fragments. The disruption of lys2 was confirmed by Southern blot analysis of three different lysine auxotrophs obtained by a single crossing over or gene replacement. Thelys2-disrupted mutants lacked α-aminoadipate reductase activity (encoded by lys2) and showed specific penicillin yields double those of the parental nondisrupted strain, Wis 54-1255. The α-aminoadipic acid precursor is channelled to penicillin biosynthesis by blocking the lysine biosynthesis branch at the α-aminoadipate reductase level.

Molecular characterization of the PR-toxin gene cluster in Penicillium roqueforti and Penicillium chrysogenum: Cross talk of secondary metabolite pathways

2014 ◽  
Vol 62 ◽  
pp. 11-24 ◽  
Author(s):  
Pedro I. Hidalgo ◽  
Ricardo V. Ullán ◽  
Silvia M. Albillos ◽  
Olimpio Montero ◽  
María Ángeles Fernández-Bodega ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Molecular Characterization ◽  
Secondary Metabolite ◽  
Cross Talk ◽  
Penicillium Chrysogenum ◽  
Toxin Gene ◽  
Penicillium Roqueforti

The global regulator LaeA controls penicillin biosynthesis, pigmentation and sporulation, but not roquefortine C synthesis in Penicillium chrysogenum

Biochimie ◽  
2009 ◽  
Vol 91 (2) ◽  
pp. 214-225 ◽  
Author(s):  
Katarina Kosalková ◽  
Carlos García-Estrada ◽  
Ricardo V. Ullán ◽  
Ramiro P. Godio ◽  
Raúl Feltrer ◽  
...  
Keyword(s):  
Penicillium Chrysogenum ◽  
Penicillin Biosynthesis ◽  
Global Regulator ◽  
Roquefortine C

scholarly journals Two Components of a velvet-Like Complex Control Hyphal Morphogenesis, Conidiophore Development, and Penicillin Biosynthesis in Penicillium chrysogenum

2010 ◽  
Vol 9 (8) ◽  
pp. 1236-1250 ◽  
Author(s):  
Birgit Hoff ◽  
Jens Kamerewerd ◽  
Claudia Sigl ◽  
Rudolf Mitterbauer ◽  
Ivo Zadra ◽  
...  
Keyword(s):  
Penicillium Chrysogenum ◽  
High Performance ◽  
Strain Improvement ◽  
Bimolecular Fluorescence Complementation ◽  
Northern Hybridization ◽  
Penicillin Biosynthesis ◽  
Improvement Program ◽  
Content Type ◽  
Pellet Formation ◽  
Severe Impairment

ABSTRACT Penicillium chrysogenum is the industrial producer of the antibiotic penicillin, whose biosynthetic regulation is barely understood. Here, we provide a functional analysis of two major homologues of the velvet complex in P. chrysogenum, which we have named P. chrysogenum velA (PcvelA) and PclaeA. Data from array analysis using a ΔPcvelA deletion strain indicate a significant role of PcVelA on the expression of biosynthesis and developmental genes, including PclaeA. Northern hybridization and high-performance liquid chromatography quantifications of penicillin titers clearly show that both PcVelA and PcLaeA play a major role in penicillin biosynthesis in a producer strain that underwent several rounds of UV mutagenesis during a strain improvement program. Both regulators are further involved in different developmental processes. While PcvelA deletion leads to light-independent conidial formation, dichotomous branching of hyphae, and pellet formation in shaking cultures, a ΔPclaeA strain shows a severe impairment in conidiophore formation under both light and dark conditions. Bimolecular fluorescence complementation assays provide evidence for a velvet-like complex in P. chrysogenum, with structurally conserved components that have distinct developmental roles, illustrating the functional plasticity of these regulators in genera other than Aspergillus.

scholarly journals Molecular characterization of Penicillium chrysogenum virus: reconsideration of the taxonomy of the genus Chrysovirus

2004 ◽  
Vol 85 (7) ◽  
pp. 2111-2121 ◽  
Author(s):  
Daohong Jiang ◽  
Said A. Ghabrial
Keyword(s):  
Molecular Characterization ◽  
Penicillium Chrysogenum ◽  
Sequence Similarity ◽  
Minor Component ◽  
Amino Acid Sequences ◽  
Nucleotide Sequencing ◽  
Dsrna Segment ◽  
Cdna Clones

Molecular cloning and complete nucleotide sequencing of Penicillium chrysogenum virus (PcV) dsRNAs indicated that PcV virions contained four dsRNA segments with sizes of 3562, 3200, 2976 and 2902 bp. Each dsRNA segment had unique sequences and contained a single large open reading frame (ORF). In vitro translation of transcripts derived from full-length cDNA clones of PcV dsRNAs yielded single products of sizes similar to those predicted from the deduced amino acid sequences of the individual ORFs. Sequence similarity searches revealed that dsRNA1 encodes a putative RNA-dependent RNA polymerase. In this study, it was determined that dsRNA2 encodes the major capsid protein and that p4, encoded by dsRNA4, is virion-associated as a minor component. All four dsRNAs of PcV, like the genomic segments of viruses with multipartite genomes, were found to have extended regions of highly conserved terminal sequences at both ends. In addition to the strictly conserved 5′-terminal 10 nt, a second region consisting of reiteration of the sequence CAA was found immediately upstream of the AUG initiator codon. These (CAA) n repeats are reminiscent of the translational enhancer elements of tobamoviruses. The 3′-terminal 14 nt were also strictly conserved. As PcV and related viruses with four dsRNA segments (genus Chrysovirus) have not been previously characterized at the molecular level, they were provisionally classified in the family Partitiviridae, comprising viruses with bipartite genomes. This study represents the first report on molecular characterization of a chrysovirus and the results suggest the creation of a new family of mycoviruses with multipartite dsRNA genomes to accommodate PcV and related viruses.

Utilization of side-chain precursors for penicillin biosynthesis in a high-producing strain of Penicillium chrysogenum

1994 ◽  
Vol 40 (6) ◽  
pp. 883-887 ◽  
Author(s):  
Susanne Havn Eriksen ◽  
Bo Jensen ◽  
Ib Schneider ◽  
Svend Kaasgaard ◽  
Jørgen Olsen
Keyword(s):  
Penicillium Chrysogenum ◽  
Side Chain ◽  
Penicillin Biosynthesis
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