TY - JOUR
T1 - G6P-capturing molecules in the periplasm of Escherichia coli accelerate the shikimate pathway
AU - Fujiwara, Ryosuke
AU - Nakano, Mariko
AU - Hirata, Yuuki
AU - Otomo, Chisako
AU - Nonaka, Daisuke
AU - Kawada, Sakiya
AU - Nakazawa, Hikaru
AU - Umetsu, Mitsuo
AU - Shirai, Tomokazu
AU - Noda, Shuhei
AU - Tanaka, Tsutomu
AU - Kondo, Akihiko
N1 - Funding Information:
This work was supported by the JST-Mirai Program (Grant Number JPMJMI17EI ), Japan (to S.N. and T.T.). Additionally, it was supported by the Japan Society for the Promotion of Science ( JSPS ) Grant-in-Aid for Scientific Research (B) (Grant Number 19H02526 ), Japan (to T.T.). R.F. received support from Research Fellowship for Young Scientists from JSPS . This work was supported by the RIKEN Center for Sustainable Resource Science, Special Postdoctoral Researcher Program (to S.N.). The authors would like to thank Enago ( www.enago.jp ) for the English language review.
Publisher Copyright:
© 2022 International Metabolic Engineering Society
PY - 2022/7
Y1 - 2022/7
N2 - Escherichia coli, the most studied prokaryote, is an excellent host for producing valuable chemicals from renewable resources as it is easy to manipulate genetically. Since the periplasmic environment can be easily controlled externally, elucidating how the localization of specific proteins or small molecules in the periplasm affects metabolism may lead to bioproduction development using E. coli. We investigated metabolic changes and its mechanisms occurring when specific proteins are localized to the E. coli periplasm. We found that the periplasmic localization of β-glucosidase promoted the shikimate pathway involved in the synthesis of aromatic chemicals. The periplasmic localization of other proteins with an affinity for glucose-6-phosphate (G6P), such as inactivated mutants of Pgi, Zwf, and PhoA, similarly accelerated the shikimate pathway. Our results indicate that G6P is transported from the cytoplasm to the periplasm by the glucose transporter protein EIICBGlc, and then captured by β-glucosidase.
AB - Escherichia coli, the most studied prokaryote, is an excellent host for producing valuable chemicals from renewable resources as it is easy to manipulate genetically. Since the periplasmic environment can be easily controlled externally, elucidating how the localization of specific proteins or small molecules in the periplasm affects metabolism may lead to bioproduction development using E. coli. We investigated metabolic changes and its mechanisms occurring when specific proteins are localized to the E. coli periplasm. We found that the periplasmic localization of β-glucosidase promoted the shikimate pathway involved in the synthesis of aromatic chemicals. The periplasmic localization of other proteins with an affinity for glucose-6-phosphate (G6P), such as inactivated mutants of Pgi, Zwf, and PhoA, similarly accelerated the shikimate pathway. Our results indicate that G6P is transported from the cytoplasm to the periplasm by the glucose transporter protein EIICBGlc, and then captured by β-glucosidase.
KW - Escherichia coli
KW - Glucose-6-phosphate
KW - Periplasm
KW - Phosphotransferase system
KW - Shikimate pathway
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U2 - 10.1016/j.ymben.2022.03.002
DO - 10.1016/j.ymben.2022.03.002
M3 - Article
C2 - 35257866
AN - SCOPUS:85125760390
SN - 1096-7176
VL - 72
SP - 68
EP - 81
JO - Metabolic Engineering
JF - Metabolic Engineering
ER -
