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

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 phosphoryl...

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Main Authors:	Makino, Yuki, Sato, Takaaki, Kawamura, Hiroki, Hachisuka, Shin-ichi, Takeno, Ryo, Imanaka, Tadayuki, Atomi, Haruyuki
Format:	Online
Language:	English
Published:	Nature Publishing Group 2016
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5120207/

id	pubmed-5120207
recordtype	oai_dc
spelling	pubmed-51202072017-01-13 An archaeal ADP-dependent serine kinase involved in cysteine biosynthesis and serine metabolism Makino, Yuki Sato, Takaaki Kawamura, Hiroki Hachisuka, Shin-ichi Takeno, Ryo Imanaka, Tadayuki Atomi, Haruyuki Article 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. Nature Publishing Group 2016-11-18 /pmc/articles/PMC5120207/ /pubmed/27857065 http://dx.doi.org/10.1038/ncomms13446 Text en Copyright © 2016, The Author(s) http://creativecommons.org/licenses/by/4.0/ 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/
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Makino, Yuki Sato, Takaaki Kawamura, Hiroki Hachisuka, Shin-ichi Takeno, Ryo Imanaka, Tadayuki Atomi, Haruyuki
spellingShingle	Makino, Yuki Sato, Takaaki Kawamura, Hiroki Hachisuka, Shin-ichi Takeno, Ryo Imanaka, Tadayuki Atomi, Haruyuki An archaeal ADP-dependent serine kinase involved in cysteine biosynthesis and serine metabolism
author_facet	Makino, Yuki Sato, Takaaki Kawamura, Hiroki Hachisuka, Shin-ichi Takeno, Ryo Imanaka, Tadayuki Atomi, Haruyuki
author_sort	Makino, Yuki
title	An archaeal ADP-dependent serine kinase involved in cysteine biosynthesis and serine metabolism
title_short	An archaeal ADP-dependent serine kinase involved in cysteine biosynthesis and serine metabolism
title_full	An archaeal ADP-dependent serine kinase involved in cysteine biosynthesis and serine metabolism
title_fullStr	An archaeal ADP-dependent serine kinase involved in cysteine biosynthesis and serine metabolism
title_full_unstemmed	An archaeal ADP-dependent serine kinase involved in cysteine biosynthesis and serine metabolism
title_sort	archaeal adp-dependent serine kinase involved in cysteine biosynthesis and serine metabolism
description	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.
publisher	Nature Publishing Group
publishDate	2016
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5120207/
_version_	1613737833452797952

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

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