An archaeal ADP-dependent serine kinase involved in cysteine biosynthesis and serine metabolism

Yuki Makino, Takaaki Sato, Hiroki Kawamura, Shin-ichi Hachisuka, Ryo Takeno, Tadayuki Imanaka and Haruyuki Atomi ()
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Yuki Makino: Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku
Takaaki Sato: Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku
Hiroki Kawamura: Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku
Shin-ichi Hachisuka: Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku
Ryo Takeno: Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku
Tadayuki Imanaka: JST, CREST, 7, Gobancho, Chiyoda-ku
Haruyuki Atomi: Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku

Nature Communications, 2016, vol. 7, issue 1, 1-12

Abstract: Abstract Routes for cysteine biosynthesis are still unknown in many archaea. Here we find that the hyperthermophilic archaeon Thermococcus kodakarensis generates cysteine from serine via O-phosphoserine, in addition to the classical route from 3-phosphoglycerate. The protein responsible for serine phosphorylation is encoded by TK0378, annotated as a chromosome partitioning protein ParB. The TK0378 protein utilizes ADP as the phosphate donor, but in contrast to previously reported ADP-dependent kinases, recognizes a non-sugar substrate. Activity is specific towards free serine, and not observed with threonine, homoserine and serine residues within a peptide. Genetic analyses suggest that TK0378 is involved in serine assimilation and clearly responsible for cysteine biosynthesis from serine. TK0378 homologs, present in Thermococcales and Desulfurococcales, are most likely not ParB proteins and constitute a group of kinases involved in serine utilization.

Date: 2016
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DOI: 10.1038/ncomms13446

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