- Identification of D-amino acid dehydrogenase as an upstream regulator of the autoinduction of a putative acyltransferase in Corynebacterium glutamicum
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Jung-Hoon Lee , Yong-Jae Kim , Hee-Sung Shin , Heung-Shick Lee , Shouguang Jin , Un-Hwan Ha
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J. Microbiol. 2016;54(6):432-439. Published online May 27, 2016
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DOI: https://doi.org/10.1007/s12275-016-6046-3
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 Abstract
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Expression of a putative acyltransferase encoded by NCgl-
0350 of Corynebacterium glutamicum is induced by cell-free
culture fluids obtained from stationary-phase growth of both
C. glutamicum and Pseudomonas aeruginosa, providing evidence
for interspecies communication. Here, we further confirmed
that such communication occurs by showing that acyltransferase
expression is induced by culture fluid obtained
from diverse Gram-negative and -positive bacterial strains,
including Escherichia coli, Salmonella Typhimurium, Bacillus
subtilis, Staphylococcus aureus, Mycobacterium sp. strain JC1,
and Mycobacterium smegmatis. A homologous acyltransferase
encoded by PA5238 of P. aeruginosa was also induced by
fluids obtained from P. aeruginosa as well as other bacterial
strains, as observed for NCgl0350 of C. glutamicum. Because
C. glutamicum is difficult to study using molecular approaches,
the homologous gene PA5238 of P. aeruginosa was used to
identify PA5309 as an upstream regulator of expression. A
homologous D-amino acid dehydrogenase encoded by NCgl-
2909 of C. glutamicum was cloned based on amino acid similarity
to PA5309, and its role in the regulation of NCgl0350
expression was confirmed. Moreover, NCgl2909 played positive
roles in growth of C. glutamicum. Thus, we identified a
D-amino acid dehydrogenase as an upstream regulator of the
autoinduction of a putative acyltransferase in C. glutamicum.
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Citations
Citations to this article as recorded by  - Enhanced Bacterial Growth and Gene Expression of D-Amino Acid Dehydrogenase With D-Glutamate as the Sole Carbon Source
Takeshi Naganuma, Yoshiakira Iinuma, Hitomi Nishiwaki, Ryota Murase, Kazuo Masaki, Ryosuke Nakai
Frontiers in Microbiology.2018;[Epub] CrossRef
- Analysis of cepA Encoding an Efflux Pump-like Protein in Corynebacterium glutamicum
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Soo-Yeon Sim , Eun-Ji Hong , Younhee Kim , Heung-Shick Lee
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J. Microbiol. 2014;52(4):278-283. Published online February 17, 2014
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DOI: https://doi.org/10.1007/s12275-014-3461-1
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894
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A gene encoding a homolog of purine efflux proteins of Escherichia coli and Bacillus subtilis was identified in the genome of Corynebacterium glutamicum and designated as cepA. The gene encoded a putative protein product, containing
12 transmembrane helixes, which is a typical feature of integral membrane transport proteins. To elucidate the function of the gene, we constructed a cepA deletion mutant (ΔcepA) and a cepA-overexpressing strain and analyzed their physiological characteristics. The cepA gene could be deleted with no critical effect on cell growth. However, the cell yield of a ΔcepA strain was decreased by 10% as compared to that of a strain carrying a cepA-overexpression plasmid (P180-cepA). Further analysis identified increased resistance of the P180-cepA strain to the purine analogues 6-mercaptopurine and 6-mercaptoguanine, but not to 2-aminopurine and purine nucleoside analogues. Moreover, this strain showed increased resistance to the antibiotics nalidixic acid and ampicillin. Collectively, these data suggest that cepA is a novel multidrug resistance gene and probably functions in the efflux of toxic substances from the inside of cells to the environment, thus allowing cells to reach a higher cell yield.
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Citations
Citations to this article as recorded by - Impact of exporter proteins and their engineering on the productivity of Corynebacterium
Keita Kinose, Keiko Shinoda, Hisashi Kawasaki
Applied Microbiology and Biotechnology.2025;[Epub] CrossRef - AutoBioTech─A Versatile Biofoundry for Automated Strain Engineering
Tobias Michael Rosch, Julia Tenhaef, Tim Stoltmann, Till Redeker, Dominic Kösters, Niels Hollmann, Karin Krumbach, Wolfgang Wiechert, Michael Bott, Susana Matamouros, Jan Marienhagen, Stephan Noack
ACS Synthetic Biology.2024; 13(7): 2227. CrossRef
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