Immunological detection of the mitochondrial F<sub>1</sub>‐ATPase α subunit in the matrix of rat liver peroxisomes

Cuezva, José M.; Santarén, Juán F.; González, Pedro; Valcarce, Carmen; Luis, A M; Izquierdo, José M.

doi:10.1016/0014-5793(90)81237-i

Cited by 12 publications

(13 citation statements)

References 29 publications

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“…While the role of molecular chaperones in mitochondrial biogenesis has been partially elucidated during the last few years (see above), nothing is yet known about the existence of a proteinaceous machinery in the peroxisomal matrix that could perform similar functions to those reported for mitochondrial molecular chaperones. However, results from our laboratory initially suggested that a chaperonin function in the peroxisomal matrix could be partially accomplished by the major regulatory subunit (o~-subunit) of the mitochondrial F-type ATPase (ca 57-kDa protein) [31,33,107].…”

Section: Peroxisomal Chaperones and Chaperonins?mentioning

confidence: 99%

“…Based on the immunoreactivity towards a rabbit anti-(rat liver mitochondrial FrATPase complex) serum [176], the mitochondrial F~-ATPase ~-subunit was shown to be present also in the matrix of rat liver peroxisomes [31]. This was assessed both by immunoelectron microscopy of rat liver thin sections, in which a highly specific immunolabeling of mitochondria and peroxisomes could be observed [31,33], and by Western blotting fractionated peroxisomal and mitochondrial proteins [31]. In addition, it was shown that bovine and rat liver FrATPase ~subunit sequences contain a typical carboxy-terminai type II peroxisomal targeting signal [31,33].…”

Section: Peroxisomal Chaperones and Chaperonins?mentioning

confidence: 99%

“…We will stress those aspects of mitochon- Ultrastructure of rat liver mitochondria (m) and peroxisomes (p). Thin sections of rat liver samples embedded in WestopaI-W were processed for regular transmission electron microscopy as previously described [31]. Mitochondria are defined by the following characteristics: existence of cristae, irregular shape and double membrane.…”

Section: Introductionmentioning

confidence: 99%

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Molecular chaperones and the biogenesis of mitochondria and peroxisomes

Cuezva

Flores

Liras

et al. 1993

Biology of the Cell

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A review of the proteinaceous machinery involved in protein sorting pathways and protein folding and assembly in mitochondria and peroxisomes is presented. After considering the various sorting pathways and targeting signals of mitochondrial and peroxisomal proteins, we make a comparative dissection of the protein factors involved in: i) the stabilization of cytosolic precursor proteins in a translocation competent conformation; ii) the membrane import apparatus of mitochondria and peroxisomes; iii) the processing of mitochondrial precursor proteins, and the eventual processing of certain peroxisomal precursor, in the interior of the organelles; and iv) the requirement of molecular chaperones for appropriate folding and assembly of imported proteins in the matrix of both organelles. Those aspects of mitochondrial biogenesis that have developed rapidly during the last few years, such as the requirement of molecular chaperones, are stressed in order to stimulate further parallel investigations aimed to understand the origin, biochemistry, molecular biology and pathology of peroxisomes. In this regard, a brief review of findings from our group and others is presented in which the role of the F1-ATPase alpha-subunit is pointed out as a molecular chaperone of mitochondria and chloroplasts. In addition, data are presented that could question our previous indication that the immunoreactive protein found in the rat liver peroxisomes is due to the presence of the F1-ATPase alpha-subunit.

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Section: Peroxisomal Chaperones and Chaperonins?mentioning

confidence: 99%

Section: Peroxisomal Chaperones and Chaperonins?mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Molecular chaperones and the biogenesis of mitochondria and peroxisomes

Cuezva

Flores

Liras

et al. 1993

Biology of the Cell

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“…Some mitochondria were likely isolated with the nuclear fraction in both experiments as evidenced by the presence of an α and a β polypeptide of the F1 part of ATP synthase (table 1). ATP synthases are mitochondrial proteins although they have been identified in peroxisomes [21] and in the plasma membrane [22]. We did not identify other mitochondrial proteins that would lend support to the view that there was contamination.…”

Section: Discussionmentioning

confidence: 48%

Analysis of the Golden Syrian Hamster Anterior Pituitary Gland Proteome by Ion Trap Mass Spectrometry

Blake

Kakhniashvili²,

Goodman³

2004

Neuroendocrinology

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We utilized mass spectrometry (MS) and bioinformatics to investigate the proteome of the anterior pituitary gland (AP). Subcellular fractions of APs from 2-month-old male Golden Syrian hamsters were prepared for protein denaturation, treatment with trypsin and analyses utilizing micro liquid chromatography MS/MS and the database search software SEQUEST. In the nuclear, non-nuclear 100,000 × g and cytosolic fractions we identified 76, 52 and 52 different proteins, respectively. A total of 145 distinct proteins were detected. We identified growth hormone, prolactin, pro-opiomelanocortin, the α-subunit for the glycoprotein hormones, luteinizing hormone-β and follicle-stimulating hormone-β. Groups of other identified proteins included hormone processing, secretion granule associated, non-hormonal endoplasmic reticulum associated, calcium binding, protein kinase C associated histone and non-histone chromosomal material, other RNA-binding, splicing factors, heterogeneous nuclear ribonucleoproteins, helicases, lamins, microfilament associated, microtubule associated, adenosine triphosphate and guanosine diphosphate associated, keratins, lysosomal, ribosomal, enzymes in glycolysis and the tricarboxylic and pentose phosphate paths, glutathione associated, transmethylation, catabolic and unknown protein products as well as blood hemoglobins. Proteins previously not reported in the AP, such as fertility protein SP22, were identified. The proteins identified in the present study form a foundation for defining the proteome in normal adult male AP.

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“…A similar distribution has been described for the ␣ subunit of the F 1 -ATPase (46). In the context of a possible transduction of a Ca 2ϩ signal to the inside of peroxisomes and mitochondria this could lead to coordinated action of both organelles.…”

Section: Discussionmentioning

confidence: 72%

Molecular cloning of a peroxisomal Ca ²⁺ -dependent member of the mitochondrial carrier superfamily

Weber

Minestrini

Dyer

et al. 1997

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

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A cDNA from a novel Ca 2؉ -dependent member of the mitochondrial solute carrier superfamily was isolated from a rabbit small intestinal cDNA library. The full-length cDNA clone was 3,298 nt long and coded for a protein of 475 amino acids, with four elongation factor-hand motifs located in the N-terminal half of the molecule. The 25-kDa N-terminal polypeptide was expressed in Escherichia coli, and it was demonstrated that it bound Ca 2؉ , undergoing a reversible and specific conformational change as a result. The conformation of the polypeptide was sensitive to Ca 2؉ which was bound with high affinity (K d Ϸ 0.37 M), the apparent Hill coefficient for Ca 2؉ -induced changes being about 2.0. The deduced amino acid sequence of the C-terminal half of the molecule revealed 78% homology to Grave disease carrier protein and 67% homology to human ADP͞ATP translocase; this sequence homology identified the protein as a new member of the mitochondrial transporter superfamily. Northern blot analysis revealed the presence of a single transcript of about 3,500 bases, and low expression of the transporter could be detected in the kidney but none in the liver. The main site of expression was the colon with smaller amounts found in the small intestine proximal to the ileum. Immunoelectron microscopy localized the transporter in the peroxisome, although a minor fraction was found in the mitochondria. The Ca 2؉ binding N-terminal half of the transporter faces the cytosol.Peroxisomes and mitochondria are the two organelles present in mammalian eukaryotic cells for which an evolutionary endosymbiotic origin has been proposed (1, 2). Both organelles share a set of similar metabolic pathways, are the site of cellular oxygen consumption, and have similar macromolecular components and membrane phospholipid compositions (3). Mitochondria, in contrast to peroxisomes contain their own DNA and are surrounded by a double membrane rather than a single one. Despite the existence of mitochondrial DNA, most proteins are coded for by nuclear genes, synthesized on free cytosolic polysomes and subsequently posttranslationally sorted to their final mitochondrial location (for a review, see ref. 4). In principle, the same applies for peroxisomal proteins although much less is known about protein import in this organelle (for a review, see ref. 5).The mitochondrial inner membrane contains three different major classes of proteins: the electron transport chain complex, the ATP synthase complex, and the mitochondrial solute carriers. The first two complexes originated at the prokariotic level whereas the mitochondrial solute carriers must have developed when the ancestor prokaryote became symbiotic in the eukaryotic cell as they fulfill a new demand of the eukaryote for intensive traffic of metabolites between the cytosolic and matrix space (6

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Immunological detection of the mitochondrial F₁‐ATPase α subunit in the matrix of rat liver peroxisomes

Cited by 12 publications

References 29 publications

Molecular chaperones and the biogenesis of mitochondria and peroxisomes

Molecular chaperones and the biogenesis of mitochondria and peroxisomes

Analysis of the Golden Syrian Hamster Anterior Pituitary Gland Proteome by Ion Trap Mass Spectrometry

Molecular cloning of a peroxisomal Ca ²⁺ -dependent member of the mitochondrial carrier superfamily

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Immunological detection of the mitochondrial F1‐ATPase α subunit in the matrix of rat liver peroxisomes

Cited by 12 publications

References 29 publications

Molecular chaperones and the biogenesis of mitochondria and peroxisomes

Molecular chaperones and the biogenesis of mitochondria and peroxisomes

Analysis of the Golden Syrian Hamster Anterior Pituitary Gland Proteome by Ion Trap Mass Spectrometry

Molecular cloning of a peroxisomal Ca 2+ -dependent member of the mitochondrial carrier superfamily

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Immunological detection of the mitochondrial F₁‐ATPase α subunit in the matrix of rat liver peroxisomes

Molecular cloning of a peroxisomal Ca ²⁺ -dependent member of the mitochondrial carrier superfamily