Export of Proteins from Mitochondria

Poyton, Robert O.; Sevarino, Kevin A.; McKee, Edward E.; Duhl, David J.M.; Cameron, Vicki; Goehring, Bradley

doi:10.1016/s1569-2558(09)60017-5

Cited by 5 publications

(5 citation statements)

References 119 publications

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“…Conversely, perhaps the mitochondrially encoded subunits either do not form complexes or form unstable complexes that are subject to degradation unless they are assembled with the nuclear-coded subunits. This is supported by the finding that null mutants that carry gene disruptions in the structural genes for subunits IV and VI have reduced levels of subunits I, II, and III (11) and that the rates of subunit I degradation are enhanced in a null mutant that carries a disruption in the gene for subunit VII (63).…”

Section: Discussionmentioning

confidence: 85%

“…Subunits I, II, and III are products of mitochondrial genes (COX1, COX2, and COX3, respectively) (1,6) and make up the catalytic core of the enzyme (7,8). All three of these polypeptides are translated on mitochondrial ribosomes and are inserted co-translationally into the mitochondrial inner membrane (9), a process termed mitochondrial export (10,11). Subunits IV, V, Va or Vb, VI, VII, and VIIa are encoded by nuclear COX genes (COX4, COX5a or 5b, COX6, COX7, COX8, and COX9, respectively).…”

mentioning

confidence: 99%

“…The two different pathways followed by compartmentally separated gene products, import of nuclear-encoded proteins (14) and export of mitochondrially encoded proteins (10,11), must converge at some point into an assembly pathway during the biogenesis of holocytochrome c oxidase. Although the mitochondrial import pathways have been elucidated (for review, see Ref.…”

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confidence: 99%

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A Role for Pet100p in the Assembly of Yeast Cytochrome c Oxidase

Church¹,

Goehring

Forsha

et al. 2005

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 85%

mentioning

confidence: 99%

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confidence: 99%

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A Role for Pet100p in the Assembly of Yeast Cytochrome c Oxidase

Church¹,

Goehring

Forsha

et al. 2005

Journal of Biological Chemistry

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“…A third possibility is that a protein involved in a signal-transduction pathway serves as an electron acceptor or donor for cytochrome c oxidase, and that this protein is released under hypoxic or anoxic conditions directly into the cytosol, where it activates or inactivates transcription factors that regulate the expression of hypoxic genes. Precedent for this sort of pathway comes from the fact that mitochondria export proteins and peptides (61), and that cytochrome c, which is immediately upstream of cytochrome c oxidase in the FIG. 5.…”

Section: Discussionmentioning

confidence: 99%

Oxygen sensing in yeast: Evidence for the involvement of the respiratory chain in regulating the transcription of a subset of hypoxic genes

Kwast

Burke

Staahl

et al. 1999

Proc. Natl. Acad. Sci. U.S.A.

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161

165

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Oxygen availability affects the transcription of a number of genes in nearly all organisms. Although the molecular mechanisms for sensing oxygen are not precisely known, heme is thought to play a pivotal role. Here, we address the possibility that oxygen sensing in yeast, as in mammals, involves a redox-sensitive hemoprotein. We have found that carbon monoxide (CO) completely blocks the anoxia-induced expression of two hypoxic genes, OLE1 and CYC7, partially blocks the induction of a third gene, COX5b, and has no effect on the expression of other hypoxic or aerobic genes. In addition, transition metals (Co and Ni) induce the expression of OLE1 and CYC7 in a concentration-dependent manner under aerobic conditions. These findings suggest that the redox state of an oxygen-binding hemoprotein is involved in controlling the expression of at least two hypoxic yeast genes. By using mutants deficient in each of the two major yeast CO-binding hemoproteins (cytochrome c oxidase and f lavohemoglobin), respiratory inhibitors, and cob1 and 0 mutants, we have found that the respiratory chain is involved in the anoxic induction of these two genes and that cytochrome c oxidase is likely the hemoprotein ''sensor.'' Our findings also indicate that there are at least two classes of hypoxic genes in yeast (CO sensitive and CO insensitive) and imply that multiple pathways͞mechanisms are involved in modulating the expression of hypoxic yeast genes.

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“…This indicates that the BLE protein is exported from the mitochondria in the transgenic MT-B. The putative explanations are that: within the mitochondria exists a specific protein export mechanism [25] , [26] , BLE is a small molecule of the heterologous protein (13 kD), it can be delivered outside mitochondria or out of the algae by the protein export mechanism to create Zeomycin resistance. Further detailed pathway studies will be required.…”

Section: Discussionmentioning

confidence: 99%

Stable Expression of Antibiotic-Resistant Gene ble from Streptoalloteichus hindustanus in the Mitochondria of Chlamydomonas reinhardtii

Zhang

Zhao

et al. 2012

PLoS ONE

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The mitochondrial expression of exogenous antibiotic resistance genes has not been demonstrated successfully to date, which has limited the development of antibiotic resistance genes as selectable markers for mitochondrial site-directed transformation in Chlamydomonas reinhardtii. In this work, the plasmid pBSLPNCB was constructed by inserting the gene ble of Streptoalloteichus hindustanus (Sh ble), encoding a small (14-kilodalton) protective protein into the site between TERMINVREP-Left repeats and the cob gene in a fragment of mitochondrial DNA (mtDNA) of C. reinhardtii. The fusion DNA-construct, which contained TERMINVREP-Left, Sh ble, cob, and partial nd4 sequence, were introduced into the mitochondria of the respiratory deficient dum-1 mutant CC-2654 of C. reinhardtii by biolistic particle delivery system. A large number of transformants were obtained after eight weeks in the dark. Subsequent subculture of the transformants on the selection TAP media containing 3 ìg/mL Zeomycin for 12 months resulted in genetically modified transgenic algae MT-Bs. Sequencing and Southern analyses on the mitochondrial genome of the different MT-B lines revealed that Sh ble gene had been integrated into the mitochondrial genome of C. reinhardtii. Both Western blot, using the anti-BLE monoclonal antibody, and Zeomycin tolerance analysis confirmed the presence of BLE protein in the transgenic algal cells. It indicates that the Sh ble gene can be stably expressed in the mitochondria of C. reinhardtii.

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Export of Proteins from Mitochondria

Cited by 5 publications

References 119 publications

A Role for Pet100p in the Assembly of Yeast Cytochrome c Oxidase

A Role for Pet100p in the Assembly of Yeast Cytochrome c Oxidase

Oxygen sensing in yeast: Evidence for the involvement of the respiratory chain in regulating the transcription of a subset of hypoxic genes

Stable Expression of Antibiotic-Resistant Gene ble from Streptoalloteichus hindustanus in the Mitochondria of Chlamydomonas reinhardtii

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