Developmental regulation of the plant mitochondrial matrix located HSP70 chaperone and its role in protein import

Dudley, P; Wood, Carlton; Pratt, Jon R.; Moore, Anthony L.

doi:10.1016/s0014-5793(97)01311-2

Cited by 27 publications

(9 citation statements)

References 23 publications

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“…It has long believed that MPI is an unregulated event, until recent evidence from plant studies showed that mitochondrial internalization of proteins is influenced by light-dark cycle and developmental cues (39). The next section will address the regulation of MPI in oxidative stress conditions.…”

Section: Candas and LImentioning

confidence: 99%

MnSOD in Oxidative Stress Response-Potential RegulationviaMitochondrial Protein Influx

Candas

2014

Antioxidants & Redox Signaling

276

178

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Significance: The mitochondrial antioxidant manganese superoxide dismutase (MnSOD) is encoded by genomic DNA and its dismutase function is fully activated in the mitochondria to detoxify free radical O 2 -generated by mitochondrial respiration. Accumulating evidence shows an extensive communication between the mitochondria and cytoplasm under oxidative stress. Not only is the MnSOD gene upregulated by oxidative stress, but MnSOD activity can be enhanced via the mitochondrial protein influx (MPI). Recent Advances: A cluster of MPI containing cytoplasmic/nuclear proteins, such as cyclins, cyclin-dependent kinases, and p53 interact with and alter MnSOD activity. These proteins modulate MnSOD superoxide scavenging activity via post-translational modifications in the mitochondria. In addition to well-established pathways in gene expression, recent findings suggest that MnSOD enzymatic activity can also be enhanced by phosphorylation of specific motifs in mitochondria. This review attempts to discuss the pre-and post-translational regulation of MnSOD, and how these modifications alter MnSOD activity, which induces a cell adaptive response to oxidative stress. Critical Issues: MnSOD is biologically significant to aerobic cells. Its role in protecting the cells against the deleterious effects of reactive oxygen species is evident. However, the exact network of MnSOD-associated cellular adaptive reaction to oxidative stress and its post-translational modifications, especially its enzymatic enhancement via phosphorylation, is not yet fully understood. Future Directions: The broad discussion of the multiple aspects of MnSOD regulation, including gene expression, protein modifications, and enzymatic activity, will shed light onto the unknown mechanisms that govern the prosurvival networks involved in cellular and mitochondrial adaptive response to genotoxic environment. Antioxid. Redox Signal. 20, 1599Signal. 20, -1617

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Section: Candas and LImentioning

confidence: 99%

MnSOD in Oxidative Stress Response-Potential RegulationviaMitochondrial Protein Influx

Candas

2014

Antioxidants & Redox Signaling

276

178

View full text Add to dashboard Cite

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“…, 2008). Plant mitochondrial import has been shown to be susceptible to rhythmic and developmental control, but the basis for this regulation is not known (Dudley et al. , 1997; Glaser et al.…”

Section: Introductionmentioning

confidence: 99%

“…In contrast to the import machinery itself, very little is known about the regulation of mitochondrial import (Glaser et al, 1998;Bolender et al, 2008). Plant mitochondrial import has been shown to be susceptible to rhythmic and developmental control, but the basis for this regulation is not known (Dudley et al, 1997;Glaser et al, 1998). Import of proteins into mitochondria needs to be regulated in close correlation with the developmental stage and physiological requirements.…”

Section: Introductionmentioning

confidence: 99%

Calcium depletion and calmodulin inhibition affect the import of nuclear‐encoded proteins into plant mitochondria

Kühn¹,

Bussemer²,

Chigri³

et al. 2009

The Plant Journal

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SUMMARYMany metabolic processes essential for plant viability take place in mitochondria. Therefore, mitochondrial function has to be carefully balanced in accordance with the developmental stage and metabolic requirements of the cell. One way to adapt organellar function is the alteration of protein composition. Since most mitochondrial proteins are nuclear encoded, fine-tuning of mitochondrial protein content could be achieved by the regulation of protein translocation. Here we present evidence that the import of nuclear-encoded mitochondrial proteins into plant mitochondria is influenced by calcium and calmodulin. In pea mitochondria, the calmodulin inhibitor ophiobolin A as well as the calcium ionophores A23187 and ionomycin inhibit translocation of nuclear-encoded proteins in a concentration-dependent manner, an effect that can be countered by the addition of external calmodulin or calcium, respectively. Inhibition was observed exclusively for proteins translocating into or across the inner membrane but not for proteins residing in the outer membrane or the intermembrane space. Ophiobolin A and the calcium ionophores further inhibit translocation into mitochondria with disrupted outer membranes, but their effect is not mediated via a change in the membrane potential across the inner mitochondrial membrane. Together, our results suggest that calcium/ calmodulin influences the import of a subset of mitochondrial proteins at the inner membrane. Interestingly, we could not observe any influence of ophiobolin A or the calcium ionophores on protein translocation into mitochondria of yeast, indicating that the effect of calcium/calmodulin on mitochondrial protein import might be a plant-specific trait.

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“…Although several studies reported that purified tobacco mitochondria did not import proteins [12–14], it was subsequently shown that this was due to the fact that import into isolated tobacco mitochondria occurs in a rhythmic manner [15]. Developmental regulation of protein import has been reported in pea leaf, which was proposed to be due to a reduction in the mtHSP 70 [16]. In animals, regulation of protein import has also been reported.…”

Section: Introductionmentioning

confidence: 99%

Import of precursor proteins into mitochondria from soybean tissues during development

1999

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Characterisation of the amount of protein import of the alternative oxidase (AOX) and the F A d precursor proteins (previously shown to use different import pathways) into mitochondria from developing soybean tissues indicated that they displayed different patterns. Import of the AOX declined in both cotyledon and root mitochondria with increasing age, whereas the import of the F A d into cotyledon mitochondria remained high throughout the same period. Using primary leaf mitochondria, it was evident that import of AOX remained high while it declined in cotyledon and root mitochondria. The amount of import of the AOX into mitochondria from different tissues closely matched the amount of the Tom 20 receptor.z 1999 Federation of European Biochemical Societies.

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Developmental regulation of the plant mitochondrial matrix located HSP70 chaperone and its role in protein import

Cited by 27 publications

References 23 publications

MnSOD in Oxidative Stress Response-Potential RegulationviaMitochondrial Protein Influx

MnSOD in Oxidative Stress Response-Potential RegulationviaMitochondrial Protein Influx

Calcium depletion and calmodulin inhibition affect the import of nuclear‐encoded proteins into plant mitochondria

Import of precursor proteins into mitochondria from soybean tissues during development

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