Import of proteins into yeast mitochondria: the nuclear MAS2 gene encodes a component of the processing protease that is homologous to the MAS1-encoded subunit.

Jensen, Robert E.

doi:10.1002/j.1460-2075.1988.tb03272.x

Cited by 152 publications

(78 citation statements)

References 48 publications

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“…34,36) In N. crassa, -MPP is found in both the matrix and the inner membrane, and -MPP is present in the matrix only. 35) In Blastocladiella emersonii, -MPP is found in both the matrix and the inner membrane, as in N. crassa, but -MPP is found in the inner membrane. 37) As shown in Fig.…”

Section: Discussionmentioning

confidence: 98%

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

Nagayama

Itono

Yoshida

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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We cloned and characterized a cDNA encoding the Dictyostelium discoideum subunit of mitochondrial processing peptidase (Dd-MPP). Western blot analysis of the mitochondrial subfractions revealed that Dd-MPP is located in the mitochondrial matrix and membrane, whereas Dd-MPP, another subunit of DdMPP, is located only in the matrix. Although expression of Dd-MPP mRNA is down-regulated during early development, the level of the Dd-MPP protein is constant throughout the Dictyostelium life cycle. In a transformant expressing the antisense RNA of the -MPP gene, unexpectedly, the -MPP protein increased about 1.8-fold relative to the wild type, and its mRNA increased 4.5-fold. Expression of other mitochondrial proteins, -MPP and Cox IV, was also induced. These results suggest that antisense RNA inhibition of the -MPP gene induces gene expression of mitochondrial proteins, presumably in a retrograde signaling manner. This is the pathway of the transfer of information from the mitochondria to the nucleus.

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Section: Discussionmentioning

confidence: 98%

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

Nagayama

Itono

Yoshida

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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“…For the anti-FLAG IPs, 2 g of the M2 antibody were used per 2.0 ϫ 10 7 lysed cells. For the immunostainings, the following antibodies at the indicated dilutions were used: polyclonal anti-PTP3 antibody (1:20) (22), anti-Myc (1:1000) (Invitrogen, La Jolla, CA), and anti-F 1 B antibody (27). Immunostainings were done as described by Araki et al (28).…”

Section: Methodsmentioning

confidence: 99%

Regulation of Dictyostelium Protein-tyrosine Phosphatase-3 (PTP3) through Osmotic Shock and Stress Stimulation and Identification of pp130 as a PTP3 Substrate

Gamper¹,

Kim²,

Howard³

et al. 1999

Journal of Biological Chemistry

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Osmotic shock and growth-medium stimulation of Dictyostelium cells results in rapid cell rounding, a reduction in cell volume, and a rearrangement of the cytoskeleton that leads to resistance to osmotic shock. Osmotic shock induces the activation of guanylyl cyclase, a rise in cGMP mediating the phosphorylation of myosin II, and the tyrosine phosphorylation of actin and the ϳ130-kDa protein (p130). We present data suggesting that signaling pathways leading to these different responses are, at least in part, independent. We show that a variety of stresses induce the Ser/Thr phosphorylation of the protein-tyrosine phosphatase-3 (PTP3). This modification does not alter PTP3 catalytic activity but correlates with its translocation from the cytosol to subcellular structures that co-localize to endosomal vesicles. This translocation is independent of PTP3 activity. Mutation of the catalytically essential Cys to a Ser results in inactive PTP3 that forms a stable complex with tyrosine-phosphorylated p130 (pp130) in vivo and in vitro, suggesting that PTP3 has a substrate specificity for pp130. The data suggest that stresses activate several interacting signaling pathways controlled by Ser/Thr and Tyr phosphorylation, which, along with the activation of guanylyl cyclase, mediate the ability of this organism to respond to adverse changes in the external environment.

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“…Indirect immunofluorescence microscopy using methanol or formaldehyde fixation was performed essentially as described previously (Hagan and Hyams, 1988). Microtubules were visualized with the monoclonal TAT-1 antibody (Woods et al, 1989) mitochondria were visualized with an affinity-purified rabbit antibody directed against the ␤-subunit of the mitochondrial F 1 -ATPase protein (Jensen and Yaffe, 1988).…”

Section: Microscopic Analysismentioning

confidence: 99%

Mmd1p, a Novel, Conserved Protein Essential for Normal Mitochondrial Morphology and Distribution in the Fission YeastSchizosaccharomyces pombe

Weir

Yaffe

2004

MBoC

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The mmd1 mutation causes temperature-sensitive growth and defects in mitochondrial morphology and distribution in the fission yeast Schizosaccharomyces pombe. In mutant cells, mitochondria aggregate at the two cell ends, with increased aggregation at elevated temperatures. Microtubules, which mediate mitochondrial positioning in fission yeast, seem normal in mmd1 cells at permissive temperature and after several hours at the nonpermissive temperature but display aberrant organization after prolonged periods at 37°C. Additionally, cells harboring both mmd1 and ban5-4, a temperature-sensitive allele of ␣2-tubulin, display synthetic defects in growth and mitochondrial distribution. The mmd1 mutation maps to an open reading frame encoding a novel 35.7-kDa protein. The Mmd1p sequence features repeating EZ-HEAT motifs and displays high conservation with uncharacterized homologues found in a variety of organisms. Saccharomyces cerevisiae cells depleted for their MMD1 homologue show increased sensitivity to the antimicrotubule drug benomyl, and the S. cerevisiae gene complemented the S. pombe mutation. Mmd1p was localized to the cytosol. Mmd1p is the first identified component required for the alignment of mitochondria along microtubules in fission yeast.

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Import of proteins into yeast mitochondria: the nuclear MAS2 gene encodes a component of the processing protease that is homologous to the MAS1-encoded subunit.

Cited by 152 publications

References 48 publications

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

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

Regulation of Dictyostelium Protein-tyrosine Phosphatase-3 (PTP3) through Osmotic Shock and Stress Stimulation and Identification of pp130 as a PTP3 Substrate

Mmd1p, a Novel, Conserved Protein Essential for Normal Mitochondrial Morphology and Distribution in the Fission YeastSchizosaccharomyces pombe

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