TY - JOUR
T1 - Processing and secretion of non-cognate bacteriocins by EnkT, an ABC transporter from a multiple-bacteriocin producer, Enterococcus faecium NKR-5-3
AU - Sushida, Hirotoshi
AU - Sakei, Miyuki
AU - Perez, Rodney H.
AU - Ishibashi, Naoki
AU - Zendo, Takeshi
AU - Wilaipun, Pongtep
AU - Leelawatcharamas, Vichien
AU - Nakayama, Jiro
AU - Sonomoto, Kenji
N1 - Funding Information:
This study was supported in part by the Grants-in-Aid for Scientific Research provided by the Japan Society for the Promotion of Science (JSPS KAKENHI , Grant Number JP17H03797 ) and the “Innovation inspired by Nature” Research Support Program , Sekisui Chemical Co., Ltd.
Funding Information:
This study was supported in part by the Grants-in-Aid for Scientific Research provided by the Japan Society for the Promotion of Science (JSPS KAKENHI, Grant Number JP17H03797) and the ?Innovation inspired by Nature? Research Support Program, Sekisui Chemical Co. Ltd.
Publisher Copyright:
© 2020 The Society for Biotechnology, Japan
PY - 2020/12
Y1 - 2020/12
N2 - EnkT is an ATP-binding cassette (ABC) transporter produced by Enterococcus faecium NKR-5-3, which is responsible for the secretion of multiple bacteriocins; enterocins NKR-5-3A, C, D, and Z (Ent53A, C, D, and Z). EnkT has been shown to possess a tolerant recognition mechanism that enables it to secrete the mature Ent53C from a chimeric precursor peptide containing the leader peptide moieties that are derived from different heterologous bacteriocins. In this study, to further characterize EnkT, we aimed to investigate the capacity of EnkT to recognize, process, and secrete non-cognate bacteriocins, which belong to different subclasses of class II. For this, the non-cognate bacteriocin precursor peptides, including enterocin A, pediocin PA-1, lactococcin Q, lactococcin A, and lacticin Q were co-expressed with EnkT, and thereafter, the production of the mature forms of these non-cognate bacteriocins was assessed. Our results revealed that EnkT could potentially recognize, process, and secrete the non-cognate bacteriocins with an exception of the leaderless bacteriocin, lacticin Q. Moreover, the processing and secretion efficiencies of these heterologous non-cognate bacteriocins by EnkT were further enhanced when the leader peptide moiety was replaced with the Ent53C leader peptide (derived from a native NKR-5-3 bacteriocin). The findings of this study describe the wide substrate tolerance of this ABC transporter, EnkT, that can be exploited in the future in establishing effective bacteriocin production systems adaptive to complex fermentation conditions common in many food systems.
AB - EnkT is an ATP-binding cassette (ABC) transporter produced by Enterococcus faecium NKR-5-3, which is responsible for the secretion of multiple bacteriocins; enterocins NKR-5-3A, C, D, and Z (Ent53A, C, D, and Z). EnkT has been shown to possess a tolerant recognition mechanism that enables it to secrete the mature Ent53C from a chimeric precursor peptide containing the leader peptide moieties that are derived from different heterologous bacteriocins. In this study, to further characterize EnkT, we aimed to investigate the capacity of EnkT to recognize, process, and secrete non-cognate bacteriocins, which belong to different subclasses of class II. For this, the non-cognate bacteriocin precursor peptides, including enterocin A, pediocin PA-1, lactococcin Q, lactococcin A, and lacticin Q were co-expressed with EnkT, and thereafter, the production of the mature forms of these non-cognate bacteriocins was assessed. Our results revealed that EnkT could potentially recognize, process, and secrete the non-cognate bacteriocins with an exception of the leaderless bacteriocin, lacticin Q. Moreover, the processing and secretion efficiencies of these heterologous non-cognate bacteriocins by EnkT were further enhanced when the leader peptide moiety was replaced with the Ent53C leader peptide (derived from a native NKR-5-3 bacteriocin). The findings of this study describe the wide substrate tolerance of this ABC transporter, EnkT, that can be exploited in the future in establishing effective bacteriocin production systems adaptive to complex fermentation conditions common in many food systems.
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U2 - 10.1016/j.jbiosc.2020.07.017
DO - 10.1016/j.jbiosc.2020.07.017
M3 - Article
C2 - 32855046
AN - SCOPUS:85089824648
VL - 130
SP - 596
EP - 603
JO - Journal of Bioscience and Bioengineering
JF - Journal of Bioscience and Bioengineering
SN - 1389-1723
IS - 6
ER -