Journal Article FZJ-2020-00239

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Molecular adaptations of NADP-malic enzyme for its function in C4 photosynthesis in grasses

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2019
Nature Publ. Group London

Nature plants 5(7), 755 - 765 () [10.1038/s41477-019-0451-7]

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Abstract: 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

Classification:

Contributing Institute(s):
  1. Strukturbiochemie (ICS-6)
Research Program(s):
  1. 552 - Engineering Cell Function (POF3-552) (POF3-552)

Appears in the scientific report 2019
Database coverage:
Medline ; Embargoed OpenAccess ; BIOSIS Previews ; Clarivate Analytics Master Journal List ; Current Contents - Agriculture, Biology and Environmental Sciences ; IF >= 10 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection
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ICS > ICS-6
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Open Access

 Datensatz erzeugt am 2020-01-15, letzte Änderung am 2021-01-30


Published on 2019-06-24. Available in OpenAccess from 2019-12-24.:
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