TY - JOUR
T1 - Diversified amino acid-mediated allosteric regulation of phosphoglycerate dehydrogenase for serine biosynthesis in land plants
AU - Okamura, Eiji
AU - Ohtaka, Kinuka
AU - Nishihama, Ryuichi
AU - Uchida, Kai
AU - Kuwahara, Ayuko
AU - Mochida, Keiichi
AU - Hirai, Masami Yokota
N1 - Funding Information:
This work was supported by the JSPS Grants-in-Aid for Scientific Research on Innovative Areas number JP25113010 to M.Y.H. and for Young Scientists (B) number JP26870855 to E.O.
Publisher Copyright:
© 2021 The Author(s).
PY - 2021/6
Y1 - 2021/6
N2 - The phosphorylated pathway of serine biosynthesis is initiated with 3-phosphoglycerate dehydrogenase (PGDH). The liverwort Marchantia polymorpha possesses an amino acidsensitive MpPGDH which is inhibited by L-serine and activated by five proteinogenic amino acids, while the eudicot Arabidopsis thaliana has amino acid-sensitive AtPGDH1 and AtPGDH3 as well as amino acid-insensitive AtPGDH2. In this study, we analyzed PGDH isozymes of the representative land plants: The monocot Oryza sativa (OsPGDH1- 3), basal angiosperm Amborella trichopoda (AmtriPGDH1-2), and moss Physcomitrium (Physcomitrella) patens (PpPGDH1-4). We demonstrated that OsPGDH1, AmtriPGDH1, PpPGDH1, and PpPGDH3 were amino acid-sensitive, whereas OsPGDH2, OsPGDH3, AmtriPGDH2, PpPGDH2, and PpPGDH4 were either sensitive to only some of the six effector amino acids or insensitive to all effectors. This indicates that PGDH sensitivity to effectors has been diversified among isozymes and that the land plant species examined, except for M. polymorpha, possess different isozyme types in terms of regulation. Phylogenetic analysis suggested that the different sensitivities convergently evolved in the bryophyte and angiosperm lineages. Site-directed mutagenesis of AtPGDH1 revealed that Asp538 and Asn556 residues in the ACT domain are involved in allosteric regulation by the effectors. These findings provide insight into the evolution of PGDH isozymes, highlighting the functional diversification of allosteric regulation in land plants.
AB - The phosphorylated pathway of serine biosynthesis is initiated with 3-phosphoglycerate dehydrogenase (PGDH). The liverwort Marchantia polymorpha possesses an amino acidsensitive MpPGDH which is inhibited by L-serine and activated by five proteinogenic amino acids, while the eudicot Arabidopsis thaliana has amino acid-sensitive AtPGDH1 and AtPGDH3 as well as amino acid-insensitive AtPGDH2. In this study, we analyzed PGDH isozymes of the representative land plants: The monocot Oryza sativa (OsPGDH1- 3), basal angiosperm Amborella trichopoda (AmtriPGDH1-2), and moss Physcomitrium (Physcomitrella) patens (PpPGDH1-4). We demonstrated that OsPGDH1, AmtriPGDH1, PpPGDH1, and PpPGDH3 were amino acid-sensitive, whereas OsPGDH2, OsPGDH3, AmtriPGDH2, PpPGDH2, and PpPGDH4 were either sensitive to only some of the six effector amino acids or insensitive to all effectors. This indicates that PGDH sensitivity to effectors has been diversified among isozymes and that the land plant species examined, except for M. polymorpha, possess different isozyme types in terms of regulation. Phylogenetic analysis suggested that the different sensitivities convergently evolved in the bryophyte and angiosperm lineages. Site-directed mutagenesis of AtPGDH1 revealed that Asp538 and Asn556 residues in the ACT domain are involved in allosteric regulation by the effectors. These findings provide insight into the evolution of PGDH isozymes, highlighting the functional diversification of allosteric regulation in land plants.
UR - http://www.scopus.com/inward/record.url?scp=85108436897&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85108436897&partnerID=8YFLogxK
U2 - 10.1042/BCJ20210191
DO - 10.1042/BCJ20210191
M3 - Article
C2 - 34032263
AN - SCOPUS:85108436897
VL - 478
SP - 2217
EP - 2232
JO - Biochemical Journal
JF - Biochemical Journal
SN - 0264-6021
IS - 12
ER -