Title Identification of D-amino acid dehydrogenase as an upstream regulator of the autoinduction of a putative acyltransferase in Corynebacterium glutamicum
Author Jung-Hoon Lee1, Yong-Jae Kim1, Hee-Sung Shin1, Heung-Shick Lee1, Shouguang Jin2, and Un-Hwan Ha1*
Address 1Department of Biotechnology and Bioinformatics, Korea University, Sejong 30019, Republic of Korea, 2Department of Molecular Genetics and Microbiology, University of Florida, Gainesville, FL 32610, USA
Bibliography Journal of Microbiology, 54(6),432-439, 2016,
DOI 10.1007/s12275-016-6046-3
Key Words acyltransferase, autoinduction, Corynebacterium glutamicum, D-amino acid dehydrogenase, Pseudomonas aeruginosa
Abstract 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.