Overproduction of CaStr2p native and His-tag versions.

Description

Enzyme of fungal L-methionine biosynthetic pathway: cystathionine-γ-synthase (CaStr2p) could be exploited as molecular target for antifungal chemotherapy. The goal of the study was to obtain conditions optimal for protein production with the use of prokaryotic cells. The constructed expression plasmids, designed in three different versions: encoding a native protein CaStr2p or recombinants with oligo-His tags added either at the C- (CaStr2CHp) or N-end (CaStr2NHp) were used for overexpression of the cloned genes in a IPTG inducible Tabor-Studier system.

This dataset contains the description of methodology, used E. coli cells, overproduction conditions and two image files with the results of SDS-PAGE analysis of CaStr2p, CaStr2NHp and CaStr2CHp overproduction in E. coli cells.

The studies were financially supported from the project OPUS 20 financed by the National Science Centre (No. UMO-2020/39/B/NZ7/01519).

Dataset file

Overproduction of CaStr2p native and His-tag versions.zip

1.8 MB, S3 ETag d835100aa516840df02c7ecb7f0510b8-1, downloads: 54

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Raw data:: Data contained in dataset was not processed.

Details

Year of publication:

2024

Verification date:

2024-06-05

Dataset language:

English

Fields of science:

chemical sciences (Natural sciences)

DOI:

10.34808/qykc-7t65

Funding:

Enzymes of the L-methionine biosynthetic pathway as novel molecular targets for antifungal chemotherapy

Verified by:

Gdańsk University of Technology

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