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Corynebacterium glutamicum ATCC 13032

ABSTRACT: Pupylated proteins in Corynebacterium glutamicum revealed by MudPIT analysis

PROVIDER: PRJNA208736 | ENA |

REPOSITORIES: ENA

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Exploring the secretome of Corynebacterium glutamicum ATCC 13032

Project description:The demand for alternative sources of food proteins is increasing due to the limitations and challenges associated with conventional food production. Advances in biotechnology have enabled the production of proteins using microorganisms, thus prompting the exploration of attractive microbial hosts capable of producing functional proteins in high titers. Corynebacterium glutamicum is widely used in industry for the production of amino acids and has many advantages as a host organism for recombinant protein production. However, its performance in this area is limited by low yields of target proteins and high levels of native protein secretion. Despite representing a challenge for heterologous protein production, the C. glutamicum secretome has not been fully characterized. In this study, state-of-the-art mass spectrometry-based proteomics was used to identify and analyze the proteins secreted by C. glutamicum. Both the wild-type strain and a strain that produced and secreted a recombinant ß-lactoglobulin protein were analyzed. A total of 427 proteins were identified in the culture supernatants, with 148 predicted to possess a secretion signal peptide. The top 12 most abundant proteins accounted for almost 80% of the secretome. These are uncharacterized proteins of unknown function, resuscitation promoting factors, protein PS1, Porin B, ABC-type transporter protein and hypothetical membrane protein. The data from this study can provide valuable insight for researchers looking to improve protein secretion and optimize C. glutamicum as a host for secretory protein production.

2024-01-18 | PXD047109 | Pride

Transcriptional response of Corynebacterium glutamicum ATCC 13032 to 2.5 mM indole

Project description:Differential gene expression analysis of C. glutamicum ATCC 13032 in presence of 2.5 mM indole compared to control conditions without indole. C. glutamicum ATCC 13032 cells were cultivated in CGXII minimal medium with 40 g per litre glucose in presence of 2.5 mM indole and harvested during exponential phase (o.d.600 4).

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Comparative LC/MS-based profiling of L-arginine producing, canavanine resistant Corynebacterium glutamicum strain ATCC 21831 and type strain ATCC 13032

Project description:Corynebacterium glutamicum strain ATCC 21831 is a producer of L-arginine that was created by random mutagenesis. It is resistant to the arginine structural analogue canavanine. In order to identify potential bottlenecks in the biosynthetic pathway that leads to this industrially important amino acid, relative metabolite abundances of biosynthetic intermediates were determined in comparison to the type strain ATCC 13032. An extract of U13C-labeled biomass was used as internal standard, to correct for different ionization efficiencies. Metabolites were identified using the ALLocator web platform.

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