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Title: An archaeal ADP-dependent serine kinase involved in cysteine biosynthesis and serine metabolism
Authors: Makino, Yuki
Sato, Takaaki
Kawamura, Hiroki
Hachisuka, Shin-ichi
Takeno, Ryo
Imanaka, Tadayuki
Atomi, Haruyuki  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0001-9687-6426 (unconfirmed)
Author's alias: 佐藤, 喬章
跡見, 晴幸
Keywords: Archaeal physiology
Kinases
Issue Date: 18-Nov-2016
Publisher: Springer Nature
Journal title: Nature Communications
Volume: 7
Thesis number: 13446
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.
Rights: © The Author(s) 2016.
This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
URI: http://hdl.handle.net/2433/226280
DOI(Published Version): 10.1038/ncomms13446
PubMed ID: 27857065
Appears in Collections:Journal Articles

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