Characterization of a farnesyl diphosphate synthase gene from Penicillium brevicompactum MUCL 19011

OBJECTIVES: Farnesyl diphosphate synthase is a critical enzyme in the isoprenoids biosynthesis pathway responsible for ergosterol and secondary metabolites biosynthesis in fungi. RESULTS: Characterization of fds from Penicillium brevicompactum (Pbfds) was performed using TAIL-PCR and RT-PCR followed...

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Veröffentlicht in:Biotechnology letters 2016-01, Vol.38 (1), p.71-79
Hauptverfasser: Sharifirad, Atefeh, Mohammadian, Somayeh, Yakhchali, Bagher, Mehrpooyan, Sina, Fatemi, Seyed Safa-ali
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container_issue 1
container_start_page 71
container_title Biotechnology letters
container_volume 38
creator Sharifirad, Atefeh
Mohammadian, Somayeh
Yakhchali, Bagher
Mehrpooyan, Sina
Fatemi, Seyed Safa-ali
description OBJECTIVES: Farnesyl diphosphate synthase is a critical enzyme in the isoprenoids biosynthesis pathway responsible for ergosterol and secondary metabolites biosynthesis in fungi. RESULTS: Characterization of fds from Penicillium brevicompactum (Pbfds) was performed using TAIL-PCR and RT-PCR followed by complementation tests in Saccharomyces cerevisiae and determination of its expression profile by semi-quantitative RT-PCR. Promoter analysis suggests some binding sites for transcription factors some of which are involved in fungal growth and response to environmental stress. The Pbfds ORF encodes a cytosolic 39.7 kDa protein with a high conservation among Eurotiomycetes and the highest identity (96 %) with Pen. chrysogenum. Homology-based structural modeling suggests that the PbFDS is formed by the arrangement of 15 core helices around a large central cavity where the catalytic reaction takes place. Superimposition of the predicted 3D structure of the enzyme on its ortholog in human reveals the same folding pattern in the counterparts. CONCLUSION: The Pbfds expression may be stimulated in response to the environmental stresses and fungal growth and encodes the PBFDS—a cytosolic enzyme which with a key role in ergosterol and secondary metabolites biosynthesis.
doi_str_mv 10.1007/s10529-015-1943-9
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RESULTS: Characterization of fds from Penicillium brevicompactum (Pbfds) was performed using TAIL-PCR and RT-PCR followed by complementation tests in Saccharomyces cerevisiae and determination of its expression profile by semi-quantitative RT-PCR. Promoter analysis suggests some binding sites for transcription factors some of which are involved in fungal growth and response to environmental stress. The Pbfds ORF encodes a cytosolic 39.7 kDa protein with a high conservation among Eurotiomycetes and the highest identity (96 %) with Pen. chrysogenum. Homology-based structural modeling suggests that the PbFDS is formed by the arrangement of 15 core helices around a large central cavity where the catalytic reaction takes place. Superimposition of the predicted 3D structure of the enzyme on its ortholog in human reveals the same folding pattern in the counterparts. 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RESULTS: Characterization of fds from Penicillium brevicompactum (Pbfds) was performed using TAIL-PCR and RT-PCR followed by complementation tests in Saccharomyces cerevisiae and determination of its expression profile by semi-quantitative RT-PCR. Promoter analysis suggests some binding sites for transcription factors some of which are involved in fungal growth and response to environmental stress. The Pbfds ORF encodes a cytosolic 39.7 kDa protein with a high conservation among Eurotiomycetes and the highest identity (96 %) with Pen. chrysogenum. Homology-based structural modeling suggests that the PbFDS is formed by the arrangement of 15 core helices around a large central cavity where the catalytic reaction takes place. Superimposition of the predicted 3D structure of the enzyme on its ortholog in human reveals the same folding pattern in the counterparts. 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RESULTS: Characterization of fds from Penicillium brevicompactum (Pbfds) was performed using TAIL-PCR and RT-PCR followed by complementation tests in Saccharomyces cerevisiae and determination of its expression profile by semi-quantitative RT-PCR. Promoter analysis suggests some binding sites for transcription factors some of which are involved in fungal growth and response to environmental stress. The Pbfds ORF encodes a cytosolic 39.7 kDa protein with a high conservation among Eurotiomycetes and the highest identity (96 %) with Pen. chrysogenum. Homology-based structural modeling suggests that the PbFDS is formed by the arrangement of 15 core helices around a large central cavity where the catalytic reaction takes place. Superimposition of the predicted 3D structure of the enzyme on its ortholog in human reveals the same folding pattern in the counterparts. CONCLUSION: The Pbfds expression may be stimulated in response to the environmental stresses and fungal growth and encodes the PBFDS—a cytosolic enzyme which with a key role in ergosterol and secondary metabolites biosynthesis.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>26334936</pmid><doi>10.1007/s10529-015-1943-9</doi><tpages>9</tpages></addata></record>
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subjects Applied Microbiology
Binding Sites
Biochemistry
Biomedical and Life Sciences
Biosynthesis
Biotechnology
Chemical synthesis
Cloning, Molecular - methods
Diphosphates
Environmental stress
Enzymes
ergosterol
Fungal Proteins - chemistry
Fungal Proteins - genetics
Fungal Proteins - metabolism
Fungi
Gene Expression Profiling - methods
genes
Geranyltranstransferase - chemistry
Geranyltranstransferase - genetics
Geranyltranstransferase - metabolism
humans
isoprenoids
Life Sciences
Mathematical models
Metabolites
microbial growth
Microbiology
Models, Molecular
open reading frames
Original Research Paper
Penicillium
Penicillium - enzymology
Penicillium - genetics
Penicillium brevicompactum
Phosphates
Promoter Regions, Genetic
reverse transcriptase polymerase chain reaction
Saccharomyces cerevisiae
Secondary metabolites
Stresses
transcription factors
Transcription Factors - metabolism
title Characterization of a farnesyl diphosphate synthase gene from Penicillium brevicompactum MUCL 19011
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