Molecular engineering in plants articles within Nature

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  • Article |

    Arabidopsis thaliana UMAMIT uniporters facilitate glucosinolate efflux from biosynthetic cells along the electrochemical gradient into the apoplast, in which the high-affinity H+-coupled glucosinolate importers GLUCOSINOLATE TRANSPORTERS (GTRs) load them into the phloem for translocation to the seeds.

    • Deyang Xu
    • , Niels Christian Holm Sanden
    •  & Barbara Ann Halkier
  • Letter
    | Open Access

    Whole-genome sequencing of the seagrass Zostera, representing the first marine angiosperm genome to be fully sequenced, provides insight into the evolutionary changes associated with a transition to a marine environment in this angiosperm lineage.

    • Jeanine L. Olsen
    • , Pierre Rouzé
    •  & Yves Van de Peer
  • Letter |

    The plant enzyme Rubisco is the main enzyme converting atmospheric carbon dioxide into biological compounds, however, this enzymatic process is inefficient in vascular plants; this study demonstrates that tobacco plants can be engineered to fix carbon with a faster cyanobacterial Rubisco, thus potentially improving plant photosynthesis.

    • Myat T. Lin
    • , Alessandro Occhialini
    •  & Maureen R. Hanson
  • Letter |

    A gene that is present in phosphate-deficiency-tolerant rice but absent from modern rice varieties is characterized and named phosphorus-starvation tolerance 1 (PSTOL1); overexpression of PSTOL1 in rice species that naturally lack this gene confers tolerance to low phosphorus conditions, a finding that may have implications for agricultural productivity in rice-growing countries.

    • Rico Gamuyao
    • , Joong Hyoun Chin
    •  & Sigrid Heuer
  • Article |

    Form I Rubisco, one of the most abundant proteins in nature, catalyses the fixation of atmospheric CO2 in photosynthesis. The limited catalytic efficiency of Rubisco has sparked extensive efforts to re-engineer the enzyme to enhance agricultural productivity. To bring this goal closer, the formation of cyanobacterial form I Rubisco is now analysed by in vitro reconstitution and cryo-electron microscopy.

    • Cuimin Liu
    • , Anna L. Young
    •  & Manajit Hayer-Hartl