Literature DB >> 29758131

The outer membrane Omp85-like protein P39 influences metabolic homeostasis in mature Arabidopsis thaliana.

Y-C Hsueh1, K Nicolaisen1, L E Gross1, J Nöthen1,2, N Schauer3, L Vojta4, F Ertel1, I Koch2, R Ladig1, H Fulgosi4, A R Fernie3, E Schleiff1,5,6.   

Abstract

The Omp85 proteins form a large membrane protein family in bacteria and eukaryotes. Omp85 proteins are composed of a C-terminal β-barrel-shaped membrane domain and one or more N-terminal polypeptide transport-associated (POTRA) domains. However, Arabidopsis thaliana contains two genes coding for Omp85 proteins without a POTRA domain. One gene is designated P39, according to the molecular weight of the encoded protein. The protein is targeted to plastids and it was established that p39 has electrophysiological properties similar to other Omp85 family members, particularly to that designated as Toc75V/Oep80. We analysed expression of the gene and characterised two T-DNA insertion mutants, focusing on alterations in photosynthetic activity, plastid ultrastructure, global expression profile and metabolome. We observed pronounced expression of P39, especially in veins. Mutants of P39 show growth aberrations, reduced photosynthetic activity and changes in plastid ultrastructure, particularly in the leaf tip. Further, they display global alteration of gene expression and metabolite content in leaves of mature plants. We conclude that the function of the plastid-localised and vein-specific Omp85 family protein p39 is important, but not essential, for maintenance of metabolic homeostasis of full-grown A. thaliana plants. Further, the function of p39 in veins influences the functionality of other plant tissues. The link connecting p39 function with metabolic regulation in mature A. thaliana is discussed.
© 2018 German Society for Plant Sciences and The Royal Botanical Society of the Netherlands.

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Keywords:  zzm321990Arabidopsis thalianazzm321990; Omp85; chloroplasts; metabolism; vein

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Year:  2018        PMID: 29758131     DOI: 10.1111/plb.12839

Source DB:  PubMed          Journal:  Plant Biol (Stuttg)        ISSN: 1435-8603            Impact factor:   3.081


  2 in total

1.  Insertion of plastidic β-barrel proteins into the outer envelopes of plastids involves an intermembrane space intermediate formed with Toc75-V/OEP80.

Authors:  Lucia E Gross; Anna Klinger; Nicole Spies; Theresa Ernst; Nadine Flinner; Stefan Simm; Roman Ladig; Uwe Bodensohn; Enrico Schleiff
Journal:  Plant Cell       Date:  2021-07-02       Impact factor: 11.277

2.  Toc75-V/OEP80 is processed during translocation into chloroplasts, and the membrane-embedded form exposes its POTRA domain to the intermembrane space.

Authors:  Lucia E Gross; Nicole Spies; Stefan Simm; Enrico Schleiff
Journal:  FEBS Open Bio       Date:  2020-02-17       Impact factor: 2.693

  2 in total

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