TY - JOUR
T1 - Form III RubisCO-mediated transaldolase variant of the Calvin cycle in a chemolithoautotrophic bacterium
AU - Frolov, Evgenii N.
AU - Kublanov, Ilya V.
AU - Toshchakov, Stepan V.
AU - Lunev, Evgenii A.
AU - Pimenov, Nikolay V.
AU - Bonch-Osmolovskaya, Elizaveta A.
AU - Lebedinsky, Alexander V.
AU - Chernyh, Nikolay A.
N1 - Publisher Copyright:
© 2019 National Academy of Sciences. All rights reserved.
PY - 2019/9/10
Y1 - 2019/9/10
N2 - The Calvin–Benson–Bassham (CBB) cycle assimilates CO2 for the primary production of organic matter in all plants and algae, as well as in some autotrophic bacteria. The key enzyme of the CBB cycle, ribulose-bisphosphate carboxylase/oxygenase (RubisCO), is a main determinant of de novo organic matter production on Earth. Of the three carboxylating forms of RubisCO, forms I and II participate in autotrophy, and form III so far has been associated only with nucleotide and nucleoside metabolism. Here, we report that form III RubisCO functions in the CBB cycle in the thermophilic chemolithoautotrophic bacterium Thermodesulfobium acidiphilum, a phylum-level lineage representative. We further show that autotrophic CO2 fixation in T. acidiphilum is accomplished via the transaldolase variant of the CBB cycle, which has not been previously demonstrated experimentally and has been considered unlikely to occur. Thus, this work reveals a distinct form of the key pathway of CO2 fixation.
AB - The Calvin–Benson–Bassham (CBB) cycle assimilates CO2 for the primary production of organic matter in all plants and algae, as well as in some autotrophic bacteria. The key enzyme of the CBB cycle, ribulose-bisphosphate carboxylase/oxygenase (RubisCO), is a main determinant of de novo organic matter production on Earth. Of the three carboxylating forms of RubisCO, forms I and II participate in autotrophy, and form III so far has been associated only with nucleotide and nucleoside metabolism. Here, we report that form III RubisCO functions in the CBB cycle in the thermophilic chemolithoautotrophic bacterium Thermodesulfobium acidiphilum, a phylum-level lineage representative. We further show that autotrophic CO2 fixation in T. acidiphilum is accomplished via the transaldolase variant of the CBB cycle, which has not been previously demonstrated experimentally and has been considered unlikely to occur. Thus, this work reveals a distinct form of the key pathway of CO2 fixation.
KW - CBB cycle
KW - Form III RubisCO
KW - Thermodesulfobium acidiphilum
KW - Transaldolase
UR - https://www.scopus.com/pages/publications/85072046385
U2 - 10.1073/pnas.1904225116
DO - 10.1073/pnas.1904225116
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C2 - 31451656
AN - SCOPUS:85072046385
SN - 0027-8424
VL - 116
SP - 18638
EP - 18646
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 37
ER -