Removal of phosphoglycolate in hyperthermophilic archaea

作者：Yuta Michimori, Rikihisa Izaki, Yu Su, Yuto Fukuyama, Shigeru Shimamura, Karin Nishimura, Yuya Miwa, Sotaro Hamakita, Takahiro Shimosaka, Yuki Makino, Ryo Takeno, Takaaki Sato, Haruki Beppu, Isaac Cann, Tamotsu Kanai, Takuro Nunoura, Haruyuki Atomi · 发表于：Proceedings of the National Academy of Sciences · 年份：2024 · DOI：10.1073/pnas.2311390121 · 被引用次数：8 · 研究领域：Enzyme Structure and Function、Microbial Community Ecology and Physiology、Methane Hydrates and Related Phenomena

Many organisms that utilize the Calvin–Benson–Bassham (CBB) cycle for autotrophic growth harbor metabolic pathways to remove and/or salvage 2-phosphoglycolate, the product of the oxygenase activity of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). It has been presumed that the occurrence of 2-phosphoglycolate salvage is linked to the CBB cycle, and in particular, the C2 pathway to the CBB cycle and oxygenic photosynthesis. Here, we examined 2-phosphoglycolate salvage in the hyperthermophilic archaeon Thermococcus kodakarensis , an obligate anaerobe that harbors a Rubisco that functions in the pentose bisphosphate pathway. T. kodakarensis harbors enzymes that have the potential to convert 2-phosphoglycolate to glycine and serine, and their genes were identified by biochemical and/or genetic analyses. 2-phosphoglycolate phosphatase activity increased 1.6-fold when cells were grown under microaerobic conditions compared to anaerobic conditions. Among two candidates, TK1734 encoded a phosphatase specific for 2-phosphoglycolate, and the enzyme was responsible for 80% of the 2-phosphoglycolate phosphatase activity in T. kodakarensis cells. The TK1734 disruption strain displayed growth impairment under microaerobic conditions, which was relieved upon addition of sodium sulfide. In addition, glycolate was detected in the medium when T. kodakarensis was grown under microaerobic conditions. The results suggest that T. kodakarensis removes 2-phosphoglycolate via a phosphatas...