Transcriptome/Proteome Analysis of Corynebacterium glutamicum

AbstractIn this study, we provide a comprehensive analysis of the genomic features of the phage CL31 and the infection dynamics with the biotechnologically relevant host strain Corynebacterium glutamicum ATCC 13032. Genome sequencing and annotation of CL31 revealed a 45-kbp genome composed of 72 open reading frames, mimicking the GC content of its host strain (54.4 %). An ANI-based distance matrix showed the highest similarity of CL31 to the temperate corynephage Φ16. While the C. glutamicum ATCC 13032 wild type strain showed only mild propagation of CL31, a strain lacking the cglIR-cglIIR-cglIM restriction-modification system was efficiently infected by this phage. Interestingly, the prophage-free strain C. glutamicum MB001 featured an even accelerated amplification of CL31 compared to the Δresmod strain suggesting a role of cryptic prophage elements in phage defense. Proteome analysis of purified phage particles and transcriptome analysis provide important insights into structural components of the phage and the response of C. glutamicum to CL31 infection. Isolation and sequencing of CL31-resistant strains revealed SNPs in genes involved in mycolic acid biosynthesis suggesting a role of this cell envelope component in phage adsorption. Altogether, these results provide an important basis for further investigation of phage-host interactions in this important biotechnological model organism.

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A proteome analysis of the cadmium and mercury response in Corynebacterium glutamicum

PROTEOMICS ◽

10.1002/pmic.200800165 ◽

2008 ◽

Vol 8 (23-24) ◽

pp. 4976-4986 ◽

Cited By ~ 31

Author(s):

Ali Fanous ◽

Walter Weiss ◽

Angelika Görg ◽

Fritz Jacob ◽

Harun Parlar

Keyword(s):

Corynebacterium Glutamicum ◽

Proteome Analysis

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Heat Shock Proteome Analysis of Wild-Type Corynebacterium glutamicum ATCC 13032 and a Spontaneous Mutant Lacking GroEL1, a Dispensable Chaperone

Journal of Bacteriology ◽

10.1128/jb.187.3.884-889.2005 ◽

2005 ◽

Vol 187 (3) ◽

pp. 884-889 ◽

Cited By ~ 37

Author(s):

Carlos Barreiro ◽

Eva González-Lavado ◽

Sven Brand ◽

Andreas Tauch ◽

Juan F. Martín

Keyword(s):

Heat Shock ◽

Corynebacterium Glutamicum ◽

Proteome Analysis ◽

Peptide Mass Fingerprinting ◽

Start Codon ◽

Northern Analysis ◽

Spontaneous Mutant ◽

Wild Type ◽

Peptide Mass ◽

Heat Response

ABSTRACT Proteome analysis of Corynebacterium glutamicum ATCC 13032 showed that levels of several proteins increased drastically in response to heat shock. These proteins were identified as DnaK, GroEL1, GroEL2, ClpB, GrpE, and PoxB, and their heat response was in agreement with previous transcriptomic results. A major heat-induced protein was absent in the proteome of strain 13032B of C. glutamicum, used for genome sequencing in Germany, compared with the wild-type ATCC 13032 strain. The missing protein was identified as GroEL1 by matrix-assisted laser desorption ionization-time of flight peptide mass fingerprinting, and the mutation was found to be due to an insertion sequence, IsCg1, that was integrated at position 327 downstream of the translation start codon of the groEL1 gene, resulting in a truncated transcript of this gene, as shown by Northern analysis. The GroEL1 chaperone is, therefore, dispensable in C. glutamicum. On the other hand, GroEL2 appears to be essential for growth. Based on these results, the role of the duplicate groEL1 and groEL2 genes is analyzed.

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A proteome analysis of Corynebacterium glutamicum after exposure to the herbicide 2,4-dichlorophenoxy acetic acid (2,4-D)

Chemosphere ◽

10.1016/j.chemosphere.2007.04.075 ◽

2007 ◽

Vol 69 (1) ◽

pp. 25-31 ◽

Cited By ~ 15

Author(s):

Ali Fanous ◽

Florian Weiland ◽

Carsten Lück ◽

Angelika Görg ◽

Albrecht Friess ◽

...

Keyword(s):

Acetic Acid ◽

Corynebacterium Glutamicum ◽

Proteome Analysis ◽

Dichlorophenoxy Acetic Acid

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Genome Sequence of the Bacteriophage CL31 and Interaction with the Host Strain Corynebacterium glutamicum ATCC 13032

Viruses ◽

10.3390/v13030495 ◽

2021 ◽

Vol 13 (3) ◽

pp. 495

Author(s):

Max Hünnefeld ◽

Ulrike Viets ◽

Vikas Sharma ◽

Astrid Wirtz ◽

Aël Hardy ◽

...

Keyword(s):

Corynebacterium Glutamicum ◽

Cell Envelope ◽

Gc Content ◽

Model Organism ◽

Proteome Analysis ◽

Distance Matrix ◽

Mycolic Acid ◽

Host Strain ◽

Modification System

In this study, we provide a comprehensive analysis of the genomic features of the phage CL31 and the infection dynamics with the biotechnologically relevant host strain Corynebacterium glutamicum ATCC 13032. Genome sequencing and annotation of CL31 revealed a 45-kbp genome composed of 72 open reading frames, mimicking the GC content of its host strain (54.4%). An ANI-based distance matrix showed the highest similarity of CL31 to the temperate corynephage Φ16. While the C. glutamicum ATCC 13032 wild type strain showed only mild propagation of CL31, a strain lacking the cglIR-cglIIR-cglIM restriction-modification system was efficiently infected by this phage. Interestingly, the prophage-free strain C. glutamicum MB001 featured an even accelerated amplification of CL31 compared to the ∆resmod strain suggesting a role of cryptic prophage elements in phage defense. Proteome analysis of purified phage particles and transcriptome analysis provide important insights into structural components of the phage and the response of C. glutamicum to CL31 infection. Isolation and sequencing of CL31-resistant strains revealed SNPs in genes involved in mycolic acid biosynthesis suggesting a role of this cell envelope component in phage adsorption. Altogether, these results provide an important basis for further investigation of phage-host interactions in this important biotechnological model organism.

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CarR, a MarR-family regulator from Corynebacterium glutamicum, modulated antibiotic and aromatic compound resistance

Biochemical Journal ◽

10.1042/bcj20190320 ◽

2019 ◽

Vol 476 (21) ◽

pp. 3141-3159 ◽

Cited By ~ 2

Author(s):

Meiru Si ◽

Can Chen ◽

Zengfan Wei ◽

Zhijin Gong ◽

GuiZhi Li ◽

...

Keyword(s):

Stress Response ◽

Ligand Binding ◽

Corynebacterium Glutamicum ◽

Conformational Changes ◽

Cysteine Oxidation ◽

Transcriptional Regulatory ◽

Ligand Free ◽

Redox Sensing

Abstract MarR (multiple antibiotic resistance regulator) proteins are a family of transcriptional regulators that is prevalent in Corynebacterium glutamicum. Understanding the physiological and biochemical function of MarR homologs in C. glutamicum has focused on cysteine oxidation-based redox-sensing and substrate metabolism-involving regulators. In this study, we characterized the stress-related ligand-binding functions of the C. glutamicum MarR-type regulator CarR (C. glutamicum antibiotic-responding regulator). We demonstrate that CarR negatively regulates the expression of the carR (ncgl2886)–uspA (ncgl2887) operon and the adjacent, oppositely oriented gene ncgl2885, encoding the hypothetical deacylase DecE. We also show that CarR directly activates transcription of the ncgl2882–ncgl2884 operon, encoding the peptidoglycan synthesis operon (PSO) located upstream of carR in the opposite orientation. The addition of stress-associated ligands such as penicillin and streptomycin induced carR, uspA, decE, and PSO expression in vivo, as well as attenuated binding of CarR to operator DNA in vitro. Importantly, stress response-induced up-regulation of carR, uspA, and PSO gene expression correlated with cell resistance to β-lactam antibiotics and aromatic compounds. Six highly conserved residues in CarR were found to strongly influence its ligand binding and transcriptional regulatory properties. Collectively, the results indicate that the ligand binding of CarR induces its dissociation from the carR–uspA promoter to derepress carR and uspA transcription. Ligand-free CarR also activates PSO expression, which in turn contributes to C. glutamicum stress resistance. The outcomes indicate that the stress response mechanism of CarR in C. glutamicum occurs via ligand-induced conformational changes to the protein, not via cysteine oxidation-based thiol modifications.

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Proteome analysis of cerebrospinal fluid in patients with Multiple System Atrophy (MSA)

Aktuelle Neurologie ◽

10.1055/s-0028-1086803 ◽

2008 ◽

Vol 35 (S 01) ◽

Author(s):

S Werz ◽

V Lehmensiek ◽

S Süssmuth ◽

H Mogel ◽

J Brettschneider ◽

...

Keyword(s):

Cerebrospinal Fluid ◽

Multiple System Atrophy ◽

Proteome Analysis

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Protective effects of soy-isoflavones in cardiovascular disease

Hämostaseologie ◽

10.1055/s-0037-1616927 ◽

2008 ◽

Vol 28 (01/02) ◽

pp. 85-88 ◽

Cited By ~ 16

Author(s):

D. Fuchs ◽

H. Daniel ◽

U. Wenzel

Keyword(s):

Cardiovascular Disease ◽

Endothelial Cells ◽

Molecular Mechanisms ◽

Dietary Intervention ◽

Mononuclear Cells ◽

Oxidized Ldl ◽

Proteome Analysis ◽

Soy Isoflavones ◽

Protective Effects ◽

Estrogen Production

SummaryEpidemiological studies indicate that the consumption of soy-containing food may prevent or slow-down the development of cardiovascular disease. In endothelial cells application of a soy extract or a combination of the most abundant soy isoflavones genistein and daidzein both inhibited apoptosis, a driving force in atherosclerosis development, when applied in combination with oxidized LDL or homocysteine. Proteome analysis revealed that the stressorinduced alteration of protein expression profile was reversed by the soy extract or the genistein/daidzein mixture. Only few protein entities that could be functionally linked to mitochondrial dysfunction were regulated in common by both application forms of isoflavones. A dietary intervention with isoflavone-enriched soy extract in postmenopausal women, who generally show strongly increased cardiovascular risk due to diminished estrogen production, led to significant alterations in the steady state levels of proteins from mononuclear blood cells. The proteins identified by proteome analysis revealed that soy isoflavones may increase the anti-inflammatory response in blood mononuclear cells thereby contributing to the atherosclerosispreventive activities of a soy-rich diet. Conclusion: By proteome analysis protein targets were identified in vitro in endothelial cells that respond to soy isoflavones and that may decipher molecular mechanisms through which soy products exert their protective effects in the vasculature.

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