Identification of Physiological Substrates and Binding Partners of the Plant Mitochondrial Protease FTSH4 by the Trapping Approach

Opalińska, Magdalena; Parys, Katarzyna; Jańska, Hanna

doi:10.3390/ijms18112455

Cited by 15 publications

(16 citation statements)

References 44 publications

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“…Lately, Stiller et al ( 2016 ) showed that in yeast OXA translocase is essential for importing not only mitochondrially, but nuclear-encoded proteins as well. Interestingly, OXA1-like protein has been identified as a potential interaction partner of FTSH4 (Opalinska et al, 2017b ).…”

Section: Discussionmentioning

confidence: 99%

“…Our studies revealed that A. thaliana devoid of FTSH4, one of the mitochondrial inner membrane ATP-dependent proteases, displays a delay in seed germination (Gibala et al, 2009 ), however, to date no further in-depth research has been implemented to characterize molecular bases of this dysfunction and, in consequence, to define the role of FTSH4 in Arabidopsis seeds. So far, the function of the FTSH4 protease was extensively studied only during the post - germination growth phase and largely under stress conditions (Kolodziejczak et al, 2007 ; Gibala et al, 2009 ; Kicia et al, 2010 ; Zhang et al, 2014a , b ; Dolzblasz et al, 2016 ; Hong et al, 2016 ; Smakowska et al, 2016 ; Opalinska et al, 2017a , b ; Zhang et al, 2017 ). We found that a lack of FTSH4 leads to oxidative stress, a decreased activity and abundance of mitochondrial complexes I and V, a lowered amount of cardiolipin, and an alteration in protein import through the inner membrane translocase TIM17:23.…”

Section: Introductionmentioning

confidence: 99%

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Targeted Proteomics Approach Toward Understanding the Role of the Mitochondrial Protease FTSH4 in the Biogenesis of OXPHOS During Arabidopsis Seed Germination

et al. 2018

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Seed germination provides an excellent model to study the process of mitochondrial biogenesis. It is a complex and strictly regulated process which requires a proper biogenesis of fully active organelles from existing promitochondrial structures. We have previously reported that the lack of the inner mitochondrial membrane protease FTSH4 delayed Arabidopsis seed germination. Here, we implemented a targeted mass spectrometry-based approach, Multiple Reaction Monitoring (MRM), with stable-isotope-labeled standard peptides for increased sensitivity, to quantify mitochondrial proteins in dry and germinating wild-type and ftsh4 mutant seeds, lacking the FTSH4 protease. Using total seed protein extracts we measured the abundance of the peptide targets belonging to the OXPHOS complexes, AOX1A, transport, and inner membrane scaffold as well as mitochondrial proteins that are highly specific to dry and germinating seeds. The MRM assay showed that the abundance of these proteins in ftsh4 did not differ substantially from that observed in wild-type at the level of dry seed and after stratification, but we observed a reduction in protein abundance in most of the examined OXPHOS subunits in the later stages of germination. These changes in OXPHOS protein levels in ftsh4 mutants were accompanied by a lower cytochrome pathway activity as well as an increased AOX1A amount at the transcript and protein level and alternative pathway activity. The analyses of the steady-state transcript levels of mitochondrial and nuclear genes encoding OXPHOS subunits did not show significant difference in their amount, indicating that the observed changes in the OXPHOS occurred at the post-transcriptional level. At the time when ftsh4 seeds were fully germinated, the abundance of the OXPHOS proteins in the mutant was either slightly lowered or comparable to these amounts in wild-type seeds at the similar developmental stage. By the implementation of an integrative approach combining targeted proteomics, quantitative transcriptomics, and physiological studies we have shown that the FTSH4 protease has an important role in the biogenesis of OXPHOS and thus biogenesis of mitochondria during germination of Arabidopsis seeds.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Targeted Proteomics Approach Toward Understanding the Role of the Mitochondrial Protease FTSH4 in the Biogenesis of OXPHOS During Arabidopsis Seed Germination

et al. 2018

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“…Conversely, the functional relationships between i -AAA protease and other constituents of SPY complex still remain to be clarified. Interestingly, amongst proteins interacting with plant i -AAA protease, counterparts of mammalian SLP2, Slp1, and Slp2, were also identified [ 48 ].…”

Section: Molecular Architecture and Mode Of Action Of Aaa Proteasementioning

confidence: 99%

“…Across diverse species, both m -AAA and i -AAA proteases remove aberrant components of respiratory chain complexes or F 1 -F 0 ATP synthase at both sides of mitochondrial inner membrane [ 13 , 30 , 32 , 56 , 57 , 58 , 59 , 60 , 61 ]. Oxidatively damaged mitochondrial proteins arising as a result of imbalanced OXPHOS functioning can also be degraded by AAA proteases [ 48 , 60 , 62 , 63 ]. AAA proteases persistently monitor IM against superfluous subunits, whose accumulation may interfere with the assembly and activity of the complex and subsequently compromise mitochondrial function.…”

Section: Aaa Proteases Maintain Functional and Healthy Mitochondrimentioning

confidence: 99%

AAA Proteases: Guardians of Mitochondrial Function and Homeostasis

Opalińska

Jańska

2018

Cells

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Mitochondria are dynamic, semi-autonomous organelles that execute numerous life-sustaining tasks in eukaryotic cells. Functioning of mitochondria depends on the adequate action of versatile proteinaceous machineries. Fine-tuning of mitochondrial activity in response to cellular needs involves continuous remodeling of organellar proteome. This process not only includes modulation of various biogenetic pathways, but also the removal of superfluous proteins by adenosine triphosphate (ATP)-driven proteolytic machineries. Accordingly, all mitochondrial sub-compartments are under persistent surveillance of ATP-dependent proteases. Particularly important are highly conserved two inner mitochondrial membrane-bound metalloproteases known as m-AAA and i-AAA (ATPases associated with diverse cellular activities), whose mis-functioning may lead to impaired organellar function and consequently to development of severe diseases. Herein, we discuss the current knowledge of yeast, mammalian, and plant AAA proteases and their implications in mitochondrial function and homeostasis maintenance.

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“…This accumulation is an intrinsic response to the disturbed functionality of OXPHOS complexes, ineffective removal of oxidized proteins arising from reduced ATP production, and altered mitochondrial dynamics causing restricted mitophagy [ 24 ]. Recently, it was also documented that AtFTSH4 can degrade oxidatively damaged proteins in isolated mitochondria [ 27 ]. In addition, mitochondria lacking AtFTSH4 have the enhanced capacity of preprotein import through TIM17:23-dependent pathway [ 28 ].…”

Section: Introductionmentioning

confidence: 99%

Impairment of Meristem Proliferation in Plants Lacking the Mitochondrial Protease AtFTSH4

Dołzbłasz¹,

Gola²,

Sokołowska³

et al. 2018

IJMS

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Shoot and root apical meristems (SAM and RAM, respectively) are crucial to provide cells for growth and organogenesis and therefore need to be maintained throughout the life of a plant. However, plants lacking the mitochondrial protease AtFTSH4 exhibit an intriguing phenotype of precocious cessation of growth at both the shoot and root apices when grown at elevated temperatures. This is due to the accumulation of internal oxidative stress and progressive mitochondria dysfunction. To explore the impacts of the internal oxidative stress on SAM and RAM functioning, we study the expression of selected meristem-specific (STM, CLV3, WOX5) and cell cycle-related (e.g., CYCB1, CYCD3;1) genes at the level of the promoter activity and/or transcript abundance in wild-type and loss-of-function ftsh4-1 mutant plants grown at 30 °C. In addition, we monitor cell cycle progression directly in apical meristems and analyze the responsiveness of SAM and RAM to plant hormones. We show that growth arrest in the ftsh4-1 mutant is caused by cell cycle dysregulation in addition to the loss of stem cell identity. Both the SAM and RAM gradually lose their proliferative activity, but with different timing relative to CYCB1 transcriptional activity (a marker of G2-M transition), which cannot be compensated by exogenous hormones.

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Identification of Physiological Substrates and Binding Partners of the Plant Mitochondrial Protease FTSH4 by the Trapping Approach

Cited by 15 publications

References 44 publications

Targeted Proteomics Approach Toward Understanding the Role of the Mitochondrial Protease FTSH4 in the Biogenesis of OXPHOS During Arabidopsis Seed Germination

Targeted Proteomics Approach Toward Understanding the Role of the Mitochondrial Protease FTSH4 in the Biogenesis of OXPHOS During Arabidopsis Seed Germination

AAA Proteases: Guardians of Mitochondrial Function and Homeostasis

Impairment of Meristem Proliferation in Plants Lacking the Mitochondrial Protease AtFTSH4

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