4.5 Article

Genes from oxidative phosphorylation complexes II-V and two dual-function subunits of complex I are transcribed in Viscum album despite absence of the entire mitochondrial holo-complex I

Journal

MITOCHONDRION
Volume 62, Issue -, Pages 1-12

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.mito.2021.10.006

Keywords

Complex I; Gamma carbonic anhydrase; Gene expression; Mitochondrial processing protease; Mitochondrial respiratory complexes; Oxidative phosphorylation proteins; Structural modeling; Viscum album

Funding

  1. Danish Council for Independent Research \ Natural Sciences [DFF-4002-00505]
  2. Swedish National Infrastructure for Computing (SNIC) through Uppsala Multidisciplinary Center for Advanced Computational Science (UPPMAX) [SNIC 2018/8-336]

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Mistletoes such as Viscum have a unique electron transport chain with an almost complete absence of nuclear-encoded complex I genes, only expressing transcripts of two dual-function genes. Despite sequence divergence, the proteins encoded by these genes are structurally conserved. This complex I loss is a distinctive feature in Viscum species and their close relatives, making them a valuable system for studying the molecular consequences of its absence.
Mistletoes (Viscum) and close relatives are unique among flowering plants in having a drastically altered electron transport chain. Lack of complex I genes has previously been reported for the mitochondrial genome, and here we report an almost complete absence of nuclear-encoded complex I genes in the transcriptome of Viscum album. Compared to Arabidopsis with approximately 40 nuclear complex I genes, we recover only transcripts of two dual-function genes: gamma carbonic anhydrase and L-galactono-1,4-lactone dehydrogenase. The complement of genes belonging to complexes II-V of the oxidative phosphorylation pathway appears to be in accordance with other vascular plants. Additionally, transcripts encoding alternative NAD(P)H dehydrogenases and alternative oxidase were found. Despite sequence divergence, structural modeling suggests that the encoded proteins are structurally conserved. Complex I loss is a special feature in Viscum species and relatives, as all other parasitic flowering plants investigated to date seem to have a complete OXPHOS system. Hence, Viscum offers a unique system for specifically investigating molecular consequences of complex I absence, such as the role of complex I subunits involved in secondary functions.

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