TY - JOUR
T1 - Functional characterization of the phosphotransferase system in Parageobacillus thermoglucosidasius
AU - Bidart, Gonzalo N.
AU - Gharabli, Hani
AU - Welner, Ditte Hededam
N1 - Publisher Copyright:
© 2023, The Author(s).
PY - 2023
Y1 - 2023
N2 - Parageobacillus thermoglucosidasius is a thermophilic bacterium
characterized by rapid growth, low nutrient requirements, and
amenability to genetic manipulation. These characteristics along with
its ability to ferment a broad range of carbohydrates make P. thermoglucosidasius
a potential workhorse in whole-cell biocatalysis. The
phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS)
catalyzes the transport and phosphorylation of carbohydrates and sugar
derivatives in bacteria, making it important for their physiological
characterization. In this study, the role of PTS elements on the
catabolism of PTS and non-PTS substrates was investigated for P. thermoglucosidasius
DSM 2542. Knockout of the common enzyme I, part of all PTSs, showed
that arbutin, cellobiose, fructose, glucose, glycerol, mannitol,
mannose, N-acetylglucosamine, N-acetylmuramic acid,
sorbitol, salicin, sucrose, and trehalose were PTS-dependent on
translocation and coupled to phosphorylation. The role of each putative
PTS was investigated and six PTS-deletion variants could not grow on
arbutin, mannitol, N-acetylglucosamine, sorbitol, and trehalose as the main carbon source, or showed diminished growth on N-acetylmuramic acid. We concluded that PTS is a pivotal factor in the sugar metabolism of P. thermoglucosidasius
and established six PTS variants important for the translocation of
specific carbohydrates. This study lays the groundwork for engineering
efforts with P. thermoglucosidasius towards efficient utilization of diverse carbon substrates for whole-cell biocatalysis.
AB - Parageobacillus thermoglucosidasius is a thermophilic bacterium
characterized by rapid growth, low nutrient requirements, and
amenability to genetic manipulation. These characteristics along with
its ability to ferment a broad range of carbohydrates make P. thermoglucosidasius
a potential workhorse in whole-cell biocatalysis. The
phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS)
catalyzes the transport and phosphorylation of carbohydrates and sugar
derivatives in bacteria, making it important for their physiological
characterization. In this study, the role of PTS elements on the
catabolism of PTS and non-PTS substrates was investigated for P. thermoglucosidasius
DSM 2542. Knockout of the common enzyme I, part of all PTSs, showed
that arbutin, cellobiose, fructose, glucose, glycerol, mannitol,
mannose, N-acetylglucosamine, N-acetylmuramic acid,
sorbitol, salicin, sucrose, and trehalose were PTS-dependent on
translocation and coupled to phosphorylation. The role of each putative
PTS was investigated and six PTS-deletion variants could not grow on
arbutin, mannitol, N-acetylglucosamine, sorbitol, and trehalose as the main carbon source, or showed diminished growth on N-acetylmuramic acid. We concluded that PTS is a pivotal factor in the sugar metabolism of P. thermoglucosidasius
and established six PTS variants important for the translocation of
specific carbohydrates. This study lays the groundwork for engineering
efforts with P. thermoglucosidasius towards efficient utilization of diverse carbon substrates for whole-cell biocatalysis.
U2 - 10.1038/s41598-023-33918-1
DO - 10.1038/s41598-023-33918-1
M3 - Journal article
C2 - 37130962
AN - SCOPUS:85158047204
SN - 2045-2322
VL - 13
JO - Scientific Reports
JF - Scientific Reports
M1 - 7131
ER -