TY  - JOUR
AU  - Alvarez, Clarisa E.
AU  - Bovdilova, Anastasiia
AU  - Höppner, Astrid
AU  - Wolff, Christian-Claus
AU  - Saigo, Mariana
AU  - Trajtenberg, Felipe
AU  - Zhang, Tao
AU  - Buschiazzo, Alejandro
AU  - Nagel-Steger, Luitgard
AU  - Drincovich, Maria F.
AU  - Lercher, Martin J.
AU  - Maurino, Veronica G.
TI  - Molecular adaptations of NADP-malic enzyme for its function in C4 photosynthesis in grasses
JO  - Nature plants
VL  - 5
IS  - 7
SN  - 2055-0278
CY  - London
PB  - Nature Publ. Group
M1  - FZJ-2020-00239
SP  - 755 - 765
PY  - 2019
AB  - In  C4  grasses  of  agronomical  interest,  malate  shuttled  into  the  bundle  sheath  cells  is  decarboxylated  mainly  by  nicotinamide  adenine  dinucleotide  phosphate  (NADP)-malic  enzyme  (C4-NADP-ME).  The  activity  of  C4-NADP-ME  was  optimized  by  natural  selection  to  efficiently  deliver  CO2  to  Rubisco.  During  its  evolution  from  a  plastidic  non-photosynthetic  NADP-ME,  C4-NADP-ME acquired increased catalytic efficiency, tetrameric structure and pH-dependent inhibition by its substrate malate. Here,  we  identified  specific  amino  acids  important  for  these  C4  adaptions  based  on  strict  differential  conservation  of  amino  acids, combined with solving the crystal structures of maize and sorghum C4-NADP-ME. Site-directed mutagenesis and struc-tural analyses show that Q503, L544 and E339 are involved in catalytic efficiency; E339 confers pH-dependent regulation by malate, F140 is critical for the stabilization of the oligomeric structure and the N-terminal region is involved in tetramerization. Together,  the  identified  molecular  adaptations  form  the  basis  for  the  efficient  catalysis  and  regulation  of  one  of  the  central  biochemical steps in C4 metabolism
LB  - PUB:(DE-HGF)16
C6  - pmid:31235877
UR  - <Go to ISI:>//WOS:000474454600022
DO  - DOI:10.1038/s41477-019-0451-7
UR  - https://juser.fz-juelich.de/record/872761
ER  -