Functional Analysis of the Twin-Arginine Translocation Pathway in
            <i>Corynebacterium glutamicum</i>
            ATCC 13869

Kikuchi, Yoshimi; Date, Masayo; Itaya, Hiroshi; Matsui, Kunihiko; Wu, Long‐Fei

doi:10.1128/aem.01528-06

Cited by 43 publications

(31 citation statements)

References 58 publications

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“…Furthermore, the Tat-pathway-dependent secretion of GFP has been shown to be far superior in C. glutamicum compared with two other Gram-positive bacteria, Bacillus subtilis and Staphylococcus carnosus (Meissner et al, 2007). More recently, there was report of secretion of Streptococcus bovis α-amylase using cspB promoter and signal sequence by C. glutamicum for the efficient utilization of raw starch, identifying C. glutamicum as a very useful host for the expression of heterologous proteins (Kikuchi et al, 2006;Tateno and Akihiko, 2007;Kikuchi et al, 2007).…”

Section: Secretion By C Glutamicum Of Heterologous Proteinsmentioning

confidence: 99%

Prediction and analysis of the secreteomic in Corynebacterium glutamicum ATCC 13032

Hao¹,

Li²,

Yan³

et al. 2010

Afr. J. Biotechnol.

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Corynebacterium glutamicum is an outstanding organism used for amino acid production. Its ability to secrete L-glutamate has been known for almost fifty years now. The complete nucleotide sequence of C. glutamicum ATCC 13032 genome was previously determined and allowed the reliable prediction of 3056 protein-coding genes within this genome using computational methods. The 3056 open reading frames (ORFs) of C. glutamicum ATCC 13032 were used for the prediction of secreted proteins by bioinformatics approaches, such as SignalP 3.0 and Proteome Analyst. 167 proteins were predicted to be secreted and contain signal peptides, whose amino residues were relatively conserved. Among them, 10 have RR-motif signal peptide and 46 have SignalPaseII signal peptide. Total of 167 secreted proteins have functional descriptions, many of which were enzymes that are involved in metabolism. This prediction method has given good insights into the whole secreted proteome of C. glutamicum and provided basis to further studies of its secretomic features at a genome level.

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Section: Secretion By C Glutamicum Of Heterologous Proteinsmentioning

confidence: 99%

Prediction and analysis of the secreteomic in Corynebacterium glutamicum ATCC 13032

Hao¹,

Li²,

Yan³

et al. 2010

Afr. J. Biotechnol.

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“…13) The signal peptide sequence of the C. ammoniagenes CspA was used functionally to achieve heterologous protein secretion by C. glutamicum. 14,15) Recently, five or six proteins with sequence similarity to the N-terminal domain of the CspA have been found in the C. glutamicum ATCC13032 genome. 16,17) CspB was found to form the surface (S)-layer that surrounds the cell.…”

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confidence: 99%

A Role of thecspAGene Encoding a Mycolyltransferase in the Growth under Alkaline Conditions ofCorynebacterium glutamicum

Takeshita

Ito

Wachi

2010

Bioscience, Biotechnology, and Biochemistry

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“…Recently, we demonstrated that TG and human epidermal growth factor can be efficiently secreted in active forms by the C. glutamicum Sec pathway (5,6,7,19). In addition, the Tat pathway in C. glutamicum was shown to specifically mediate the secretion of Arthrobacter globiformis isomaltodextranase (IMD) (14), as well as green fluorescent protein (GFP) (30) carrying an E. coli TorA signal peptide (20,37). We also showed that pro-TG and pro-PG could be produced using the Tat pathway in C. glutamicum (20,21).…”

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confidence: 99%

“…In addition, the Tat pathway in C. glutamicum was shown to specifically mediate the secretion of Arthrobacter globiformis isomaltodextranase (IMD) (14), as well as green fluorescent protein (GFP) (30) carrying an E. coli TorA signal peptide (20,37). We also showed that pro-TG and pro-PG could be produced using the Tat pathway in C. glutamicum (20,21). More recently, Tat pathway-dependent secretion of GFP has been shown to be far more efficient in C. glutamicum than in two other gram-positive bacteria, B. subtilis and Staphylococcus carnosus (28), indicating that C. glutamicum could be a useful host for the production of heterologous proteins.…”

mentioning

confidence: 99%

“…Recently, the novel twin-arginine translocation (Tat) pathway was discovered (1,3,36); this pathway differs from the Sec pathway because it translocates folded proteins using the transmembrane proton electrochemical gradient. Various model bacterial systems have been extensively studied, including the systems of the gram-negative bacterium Escherichia coli and the gram-positive bacteria Bacillus subtilis (15,29,31), Streptomyces lividans (8,39), Mycobacterium smegmatis (27,32), and Corynebacterium glutamicum (20). The Tat pathway might have advantages over the Sec pathway for the production of heterologous proteins, because many proteins fold tightly before they reach the Sec machinery and so cannot engage with it for translocation across the cytoplasmic membrane.…”

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confidence: 99%

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TatABC Overexpression Improves Corynebacterium glutamicum Tat-Dependent Protein Secretion

Kikuchi

Itaya

Date

et al. 2009

Appl Environ Microbiol

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The twin-arginine translocation (Tat) pathway in Corynebacterium glutamicum has been described previously. The minimal functional Tat system in C. glutamicum required TatA and TatC but did not require TatB, although this component was required for maximal efficiency of Tat-dependent secretion. We previously demonstrated that Chryseobacterium proteolyticum pro-protein glutaminase (pro-PG) and Streptomyces mobaraensis pro-transglutaminase (pro-TG) could be secreted via the Tat pathway in C. glutamicum. Here we report that the amounts of pro-PG secreted were more than threefold larger when TatC or TatAC was overexpressed, and there was a further threefold increase when TatABC was overexpressed. These results show that the amount of TatC protein is the first bottleneck and the amount of TatB protein is the second bottleneck in Tat-dependent protein secretion in C. glutamicum. In addition, the amount of pro-TG that accumulated via the Tat pathway when TatABC was overexpressed with the TorA signal peptide in C. glutamicum was larger than the amount that accumulated via the Sec pathway. We concluded that TatABC overexpression improves Tat-dependent pro-PG and pro-TG secretion in C. glutamicum.Protein deamidation, which hydrolyzes the amido groups on glutamine or asparagine residues in proteins, is of great interest to the food industry because it has potential applications for improving the usefulness of a variety of food proteins (11, 41). A new protein glutaminase (PG), catalyzing the deamidation of proteins, was discovered in culture supernatants of Chryseobacterium proteolyticum (46, 47). However, the amount of PG produced by C. proteolyticum was too small for industrial applications. Streptomyces mobaraensis transglutaminase (TG) has been used in the food industry (50) to bind meat and fish and in gelled food products such as jelly, yogurt, and cheese. Moreover, this enzyme has great potential for use in the manufacture of materials found in cosmetics, thermostable microcapsules, and carriers of immobilized enzymes. Hence, there is a need to develop a more efficient system for production of TG.Extracellular protein production has several advantages over a cytoplasmic system. In many cases, the N-terminal amino acid residue of the secreted protein is identical to that of the natural protein, because the signal peptide is completely removed by a specific signal peptidase during secretion (44). In addition, due to disulfide bond formation, the correct protein conformation is more likely to occur when the enzyme is secreted, because the extracellular environment is more oxidative than the cytoplasmic environment (26). Finally, purification of a secreted protein is likely to be easier, as there are fewer contaminating proteins in the culture medium than in the cytoplasm.Most proteins secreted by bacteria are translocated across the cytoplasmic membrane by the Sec pathway, which acts on unfolded proteins using the energy provided by ATP hydrolysis (4, 33). Recently, the novel twin-arginine translocation (Tat) pathway wa...

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Functional Analysis of the Twin-Arginine Translocation Pathway in Corynebacterium glutamicum ATCC 13869

Cited by 43 publications

References 58 publications

Prediction and analysis of the secreteomic in Corynebacterium glutamicum ATCC 13032

Prediction and analysis of the secreteomic in Corynebacterium glutamicum ATCC 13032

A Role of thecspAGene Encoding a Mycolyltransferase in the Growth under Alkaline Conditions ofCorynebacterium glutamicum

TatABC Overexpression Improves Corynebacterium glutamicum Tat-Dependent Protein Secretion

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