Dataset Information

An integrative transcriptomic and proteomic analysis of an industrial clavulanic acid-overproducing Streptomyces clavuligerus

ABSTRACT: Clavulanic acid is a clinically-important secondary metabolite used in treatment of infectious diseases. We aimed to decipher complex regulatory mechanisms acting in clavulanic acid biosynthesis through the analysis of transcriptome- and proteome-wide alterations in an industrial clavulanic acid overproducer Streptomyces clavuligerus, namely DEPA and its wild-type counterpart NRRL3585.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Streptomyces Clavuligerus

SUBMITTER: Servet ÖZCAN

LAB HEAD: Servet Ozcan

PROVIDER: PXD032272 | Pride | 2022-11-02

REPOSITORIES: Pride

ACCESS DATA

Publications

An integrative-omics analysis of an industrial clavulanic acid-overproducing Streptomyces clavuligerus.

Kurt-Kızıldoğan Aslıhan A Çelik Gözde G Ünsaldı Eser E Özcan Servet S Ayaz-Güner Şerife Ş Özcengiz Gülay G

Applied microbiology and biotechnology 20220810 18

Clavulanic acid (CA) is a clinically important secondary metabolite used to treat infectious diseases. We aimed to decipher complex regulatory mechanisms acting in CA biosynthesis by analyzing transcriptome- and proteome-wide alterations in an industrial CA overproducer Streptomyces clavuligerus strain, namely DEPA and its wild-type counterpart NRRL3585. A total of 924 differentially expressed genes (DEGs) and 271 differentially produced proteins (DPPs) were obtained by RNA-seq and nanoLC-MS/MS ...[more]

PMID: 35945361

Similar Datasets

Project description:Serine proteases has been vastly reported to be found (and identified) only in seed extracts of Canavalia ensiformis (C. ensiformis), however, our group observed expressive serine protease activities in aqueous extracts from leaves, seeds, roots, and stem, especially in a leaf extract obtained with distillated water (CE-A). Additionally, this extract demonstrated very good stability in high temperatures and in the presence of chemical agents. In order to study the serine protease activity in leaves, CE-A was submitted to benzamidine-sepharose affinity column and an enriched fraction of serine proteases, named CE-ABza was purified 1.65 fold, yielding a total recovery of about 62%. Based upon zymographic analysis in a gelatin-SDS-PAGE-, the CE-ABza fraction presented an enzymatic activity band at approximately 90 kDa molecular mass region under non-reducing conditions and three bands at 17, 32 and also at 90 kDa under reducing condition. This fraction was able to hydrolyze, in a different way, peptidomimetic and protein substrates. The maximal activity was observed at basic pH values (8.0 to 9.5) and temperature about 40°C. These enzymes exhibited important thermal stability and were significantly inhibited by serine protease inhibitors, such as benzamidine and TPCK. Calcium, magnesium, manganese and zinc ions had a negative modulation on the CE-ABza activity. Mass spectrometry-based proteomics approach identified showed homology with 11 plant proteases from different legumes species, indicating their presence or demonstrating that CE-Bza proteases share specific region of the primary structure of theses enzyme, although the C. ensiformis genome and protein databases are yet to be publicly available. These results demonstrated that these molecules found in both the CE-A extract and the CE-ABza fraction presented important properties that could be used as potential pharmacological and biotechnological targets as therapeutic option. Besides, identification and characterization of C. ensiformis proteases contribute to the studies of plant enzymes.

Dataset Information

An integrative transcriptomic and proteomic analysis of an industrial clavulanic acid-overproducing Streptomyces clavuligerus

Publications

An integrative-omics analysis of an industrial clavulanic acid-overproducing Streptomyces clavuligerus.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure