Authorship：Lead author,　Corresponding author   Publishing type：Research paper (scientific journal)   Publisher：American Chemical Society (ACS)  

DOI： 10.1021/acs.biochem.3c00025

Authorship：Lead author   Publishing type：Research paper (scientific journal)   Publisher：Wiley  

DOI： 10.1002/anie.202117430

Publishing type：Research paper (scientific journal)   Publisher：American Society for Microbiology  

Serine kinase catalyzes the phosphorylation of free serine (Ser) to produce
<italic>O</italic>
-phosphoserine (Sep). An ADP-dependent Ser kinase in the hyperthermophilic archaeon
<italic>Thermococcus kodakarensis</italic>
(
<italic>Tk</italic>
-SerK) is involved in cysteine (Cys) biosynthesis and most likely Ser assimilation. An ATP-dependent Ser kinase in the mesophilic bacterium
<italic>Staphylococcus aureus</italic>
is involved in siderophore biosynthesis. Although proteins displaying various degrees of similarity with
<italic>Tk</italic>
-SerK are distributed in a wide range of organisms, it is unclear if they are actually Ser kinases. Here we examined proteins from Desulfurococcales species in Crenarchaeota that display moderate similarity with
<italic>Tk</italic>
-SerK from Euryarchaeota (42-45% identical).
<italic>Tk</italic>
-
<italic>serK</italic>
homologs from
<italic>Staphylothermus marinus</italic>
(Smar_0555),
<italic>Desulfurococcus amylolyticus</italic>
(DKAM_0858), and
<italic>Desulfurococcus mucosus</italic>
(Desmu_0904) were expressed in
<italic>Escherichia coli</italic>
. All three partially purified recombinant proteins exhibited Ser kinase activity utilizing ATP rather than ADP as a phosphate donor. Purified Smar_0555 protein displayed activity towards
<sc>l</sc>
-Ser, but not with other compounds including
<sc>d</sc>
-Ser,
<sc>l</sc>
-threonine and
<sc>l</sc>
-homoserine. The enzyme utilized ATP, UTP, GTP, CTP, and the inorganic polyphosphates triphosphate and tetraphosphate as the phosphate donor. Kinetic analysis indicated that the Smar_0555 protein preferred nucleoside 5’-triphosphates compared to triphosphate as a phosphate donor. Transcript levels and Ser kinase activity in
<italic>S. marinus</italic>
cells grown with or without serine suggested that the Smar_0555 gene is constitutively expressed. The genes encoding Ser kinases examined here form an operon with genes most likely responsible for the conversion between Sep and 3-phosphoglycerate of central sugar metabolism, suggesting that the ATP-dependent Ser kinases from Desulfurococcales play a role in the assimilation of Ser.




<bold>IMPORTANCE</bold>




Homologs of the ADP-dependent Ser kinase from the archaeon
<italic>Thermococcus kodakarensis</italic>
(
<italic>Tk</italic>
-SerK) include representatives from all three domains of life. The results of this study show that even homologs from the archaeal order Desulfurococcales, which are the most structurally related to the ADP-dependent Ser kinases from the Thermococcales, are Ser kinases that utilize ATP, and in at least some cases inorganic polyphosphates, as the phosphate donor. The differences in properties between the Desulfurococcales and Thermococcales enzymes raise the possibility that
<italic>Tk</italic>
-SerK homologs constitute a group of kinases that phosphorylate free serine with a wide range of phosphate donors.

DOI： 10.1128/jb.00025-21

Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

DOI： 10.1038/s41467-018-04201-z

Other Link： http://www.nature.com/articles/s41467-018-04201-z

Authorship：Lead author  

Authorship：Lead author,　Corresponding author   Language：Japanese  

Type：Academic society, research group, etc. 

Type：Academic society, research group, etc.