Reduced utilization of side-chain precursor for penicillin biosynthesis by mutants of Penicillium chrysogenum

1980 ◽  
Vol 2 (7) ◽  
Author(s):  
RichardC. Egen ◽  
S.G. Pathak
Keyword(s):  
Penicillium Chrysogenum ◽  
Side Chain ◽  
Penicillin Biosynthesis

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

scholarly journals Peroxisomes Are Required for Efficient Penicillin Biosynthesis in Penicillium chrysogenum

2010 ◽  
Vol 76 (17) ◽  
pp. 5702-5709 ◽  
Author(s):  
Wiebe H. Meijer ◽  
Loknath Gidijala ◽  
Susan Fekken ◽  
Jan A. K. W. Kiel ◽  
Marco A. van den Berg ◽  
...  
Keyword(s):  
Penicillium Chrysogenum ◽  
Coenzyme A ◽  
Antibiotic Production ◽  
Hyphal Growth ◽  
Side Chain ◽  
Penicillin Biosynthesis ◽  
Peroxisome Proliferation ◽  
Coa Ligase ◽  
Penicillanic Acid ◽  
Acyl Coenzyme A

ABSTRACT In the fungus Penicillium chrysogenum, penicillin (PEN) production is compartmentalized in the cytosol and in peroxisomes. Here we show that intact peroxisomes that contain the two final enzymes of PEN biosynthesis, acyl coenzyme A (CoA):6-amino penicillanic acid acyltransferase (AT) as well as the side-chain precursor activation enzyme phenylacetyl CoA ligase (PCL), are crucial for efficient PEN synthesis. Moreover, increasing PEN titers are associated with increasing peroxisome numbers. However, not all conditions that result in enhanced peroxisome numbers simultaneously stimulate PEN production. We find that conditions that lead to peroxisome proliferation but simultaneously interfere with the normal physiology of the cell may be detrimental to antibiotic production. We furthermore show that peroxisomes develop in germinating conidiospores from reticule-like structures. During subsequent hyphal growth, peroxisome proliferation occurs at the tip of the growing hyphae, after which the organelles are distributed over newly formed subapical cells. We observed that the organelle proliferation machinery requires the dynamin-like protein Dnm1.

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 ◽  
J�rgen Olsen
Keyword(s):  
Penicillium Chrysogenum ◽  
Side Chain ◽  
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.

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.

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