Antisense RNA Inhibition of the β Subunit of the<i>Dictyostelium discoideum</i>Mitochondrial Processing Peptidase Induces the Expression of Mitochondrial Proteins

Nagayama, Koki; Itono, Shiori; Yoshida, Takashi; Ishiguro, Sei-ichi; Ochiai, Hiroshi; Ohmachi, Tetsuo

doi:10.1271/bbb.80106

Cited by 17 publications

(8 citation statements)

References 49 publications

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“…Neurospora was considered to represent an intermediate stage in which a single gene encodes a bi-functional β-MPP that is shared between α-MPP to constitute a soluble MPP heterodimer and cp2 in the bc 1 complex ( Neurospora -type system) (Schulte et al 1989). A similar system was later observed also in Dictyostelium (Nagayama et al 2008). Our search across major eukaryotic groups revealed that the combined presence of α/β-MPP subunits together with cp2 known from Neurospora and Dictyostelium thus far is not an exception but that this Neurospora -type system is present in at least some members of all major eukaryotic groups.…”

Section: Discussionsupporting

confidence: 77%

An Advanced System of the Mitochondrial Processing Peptidase and Core Protein Family in Trypanosoma brucei and Multiple Origins of the Core I Subunit in Eukaryotes

Mach

Poliak

Matušková

et al. 2013

Genome Biology and Evolution

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Mitochondrial processing peptidase (MPP) consists of α and β subunits that catalyze the cleavage of N-terminal mitochondrial-targeting sequences (N-MTSs) and deliver preproteins to the mitochondria. In plants, both MPP subunits are associated with the respiratory complex bc1, which has been proposed to represent an ancestral form. Subsequent duplication of MPP subunits resulted in separate sets of genes encoding soluble MPP in the matrix and core proteins (cp1 and cp2) of the membrane-embedded bc1 complex. As only α-MPP was duplicated in Neurospora, its single β–MPP functions in both MPP and bc1 complexes. Herein, we investigated the MPP/core protein family and N-MTSs in the kinetoplastid Trypanosoma brucei, which is often considered one of the most ancient eukaryotes. Analysis of N-MTSs predicted in 336 mitochondrial proteins showed that trypanosomal N-MTSs were comparable with N-MTSs from other organisms. N-MTS cleavage is mediated by a standard heterodimeric MPP, which is present in the matrix of procyclic and bloodstream trypanosomes, and its expression is essential for the parasite. Distinct Genes encode cp1 and cp2, and in the bloodstream forms the expression of cp1 is downregulated along with the bc1 complex. Phylogenetic analysis revealed that all eukaryotic lineages include members with a Neurospora-type MPP/core protein family, whereas cp1 evolved independently in metazoans, some fungi and kinetoplastids. Evolution of cp1 allowed the independent regulation of respiration and protein import, which is essential for the procyclic and bloodstream forms of T. brucei. These results indicate that T. brucei possesses a highly derived MPP/core protein family that likely evolved in response to its complex life cycle and does not appear to have an ancient character proposed earlier for this eukaryote.

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Section: Discussionsupporting

confidence: 77%

An Advanced System of the Mitochondrial Processing Peptidase and Core Protein Family in Trypanosoma brucei and Multiple Origins of the Core I Subunit in Eukaryotes

Mach

Poliak

Matušková

et al. 2013

Genome Biology and Evolution

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“…As a sister clade to the animal and fungal lineages, it was not surprising that the core components of the TOM and TIM machinery, characterized in fungi and animals, have been identified in D. discoideum [37]–[40].…”

Section: Resultsmentioning

confidence: 99%

The Essentials of Protein Import in the Degenerate Mitochondrion of Entamoeba histolytica

et al. 2010

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Several essential biochemical processes are situated in mitochondria. The metabolic transformation of mitochondria in distinct lineages of eukaryotes created proteomes ranging from thousands of proteins to what appear to be a much simpler scenario. In the case of Entamoeba histolytica, tiny mitochondria known as mitosomes have undergone extreme reduction. Only recently a single complete metabolic pathway of sulfate activation has been identified in these organelles. The E. histolytica mitosomes do not produce ATP needed for the sulfate activation pathway and for three molecular chaperones, Cpn60, Cpn10 and mtHsp70. The already characterized ADP/ATP carrier would thus be essential to provide cytosolic ATP for these processes, but how the equilibrium of inorganic phosphate could be maintained was unknown. Finally, how the mitosomal proteins are translocated to the mitosomes had remained unclear. We used a hidden Markov model (HMM) based search of the E. histolytica genome sequence to discover candidate (i) mitosomal phosphate carrier complementing the activity of the ADP/ATP carrier and (ii) membrane-located components of the protein import machinery that includes the outer membrane translocation channel Tom40 and membrane assembly protein Sam50. Using in vitro and in vivo systems we show that E. histolytica contains a minimalist set up of the core import components in order to accommodate a handful of mitosomal proteins. The anaerobic and parasitic lifestyle of E. histolytica has produced one of the simplest known mitochondrial compartments of all eukaryotes. Comparisons with mitochondria of another amoeba, Dictystelium discoideum, emphasize just how dramatic the reduction of the protein import apparatus was after the loss of archetypal mitochondrial functions in the mitosomes of E. histolytica.

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“…PHB also serves as a mitochondrial respiratory chain chaperone protein and the decrease of PHB induces mitochondrial dysfunction and ROS overproduction (Kathiria et al, 2012). MPPB is related to mitochondrial biogenesis (Nagayama et al, 2008), and UQCRH, as a subunit of mitochondrial respiratory chain complex III (Liu et al, 2016), cooperates with SLC25A5 (ADP/ATP transport enzyme 2) to regulate ATP synthesis and transport (Clemencon et al, 2013). Classical neuropathological hallmarks of disease (Aβ and tau) may trigger mitochondrial disturbance, while mitochondrial dysfunction may incite pathology and cognitive deficits (Kerr et al, 2017; Perez Ortiz & Swerdlow, 2019).…”

Section: Discussionmentioning

confidence: 99%

Platelet biomarkers for a descending cognitive function: A proteomic approach

Liu

et al. 2021

Aging Cell

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Antisense RNA Inhibition of the β Subunit of theDictyostelium discoideumMitochondrial Processing Peptidase Induces the Expression of Mitochondrial Proteins

Cited by 17 publications

References 49 publications

An Advanced System of the Mitochondrial Processing Peptidase and Core Protein Family in Trypanosoma brucei and Multiple Origins of the Core I Subunit in Eukaryotes

An Advanced System of the Mitochondrial Processing Peptidase and Core Protein Family in Trypanosoma brucei and Multiple Origins of the Core I Subunit in Eukaryotes

The Essentials of Protein Import in the Degenerate Mitochondrion of Entamoeba histolytica

Platelet biomarkers for a descending cognitive function: A proteomic approach

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