Three-dimensional structure of the crystalloid in the microbody of Kloeckera sp.: composite crystal model

Osumi, Masako; Nagano, Misuzu; Yamada, Naoko; Hosoi, Jun; Yanagida, Mitsuhiro

doi:10.1128/jb.151.1.376-383.1982

Cited by 10 publications

(2 citation statements)

References 19 publications

(18 reference statements)

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“…Instead, catalase is located at the periphery of the organelle, at the edges of the crystalloid [58]. Hence, catalase is also not a structural part of the AO crystal as was suggested before by Osumi et al [59]. The model of Vonck and van Bruggen [57] proposes that the unit cell of 2D AO crystalloids is composed of six AO octamers, organized in three orientations, and two large holes to accommodate other proteins.…”

Section: Ao Structurementioning

confidence: 90%

Alcohol oxidase: A complex peroxisomal, oligomeric flavoprotein

Ozimek

Veenhuis

Klei

2005

FEMS Yeast Research

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Alcohol oxidase (AO) is the key enzyme of methanol metabolism in methylotrophic yeast species. It catalyses the first step of methanol catabolism, namely its oxidation to formaldehyde with concomitant production of hydrogen peroxide. In its mature active form, AO is a molecule of high molecular mass (600 kDa) that consists of eight identical subunits, each of which carry one non-covalently bound flavin adenine nucleotide (FAD) molecule as the prosthetic group. In vivo, the protein is compartmentalized into special cell organelles, termed peroxisomes. AO is an abundant protein and its synthesis is strictly regulated by repression/derepression and induction mechanisms that occur at the transcriptional level. Various aspects of its sorting and assembly/activation render AO a unique protein. Recent developments of AO synthesis, sorting and assembly/activation are highlighted in this paper.

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Section: Ao Structurementioning

confidence: 90%

Alcohol oxidase: A complex peroxisomal, oligomeric flavoprotein

Ozimek

Veenhuis

Klei

2005

FEMS Yeast Research

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“…In thin sections, however, the presence of these vesicles can be suggested because the material inside condensing vacuoles had some order indicating the presence of crystalline material. The presence of vesicles containing crystalloid material is often associated with some abnormality of metabolism or secretion (15,20,23,28). However, crystalloid granules are also present in normal a,b cells of pancreatic islets, where they function in secretory processes (28).…”

Section: Fig 2 (A)mentioning

confidence: 99%

Subcellular fractionation of a hypercellulolytic mutant, Trichoderma reesei Rut-C30: localization of endoglucanase in microsomal fraction

Glenn¹,

Ghosh²,

Ghosh³

1985

Appl Environ Microbiol

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The growing mycelia of Trichoderma reesei Rut-C30 are richly endowed with endoplasmic reticula and a variety of pleomorphic subcellular bodies. Mycelia of the culture growing in presence of avicel pHlOl was fractionated in sucrose density gradients, and several morphologically and biochemically distinct fractions were isolated. Mycelia were homogenized in a Bead Beater, and the homogenate was freed of nucleus and wall fragments by low-speed centrifugation before fractionation. Organelle-free cytosol, which did not penetrate the gradient, contained (of the total) 72% of the vanadate-sensitive ATPase, 26% of carboxymethyl cellulase (CMCase), 2% of cytochrome c reductase, and 13% of the protein. Significant fractions separated on a gradient were light vesicles containing heavily stained material inside and ribosomes attached to the outside surface, intact vesicles resembling condensing vacuoles, large vesicles derived from the plasma membrane, and heavy vesicles containing crystalline material. The light-vesicle fraction contained a large portion of the cell-bound CMCase activity. The particle-bound ATPase and cytochrome c reductase activities were concentrated in heavy fractions. The fractionation in the presence of MgCl2 improved the preservation of subcellular bodies derived from the endoplasmic reticula. Although the CMCase activity of the light-vesicle fraction was 4 times higher than the activity in the heavy-vesicle fraction, the CMCase antibody-binding capacities of both fractions were about the same. This discrepancy between the catalytic activity and the antibody-binding capacity suggests that the heavy vesicles might have contained considerable amount of inactive CMCase compared with that present in the light vesicles.

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Transmission and scanning electron microscopic examination of intracellular organelles in freeze‐substituted Kloeckera and Saccharomyces cerevisiae Yeast Cells

Baba

Osumi

1987

J. Elec. Microsc. Tech.

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Specimen preparation, Three-dimensional image KEY WORDS ABSTRACT The application of the conventional double-fixation method (glutaraldehyde and osmium tetroxide) to whole yeast cells is difficult because the thick cell wall of the yeast prevents the penetration of osmium tetroxide. However, this problem was solved by using the freeze-substitution fixation method. Therefore, it was possible to examine the intracellular structures of the yeast cells without digestion of the cell wall. In the present method, specimens for transmission electron microscopy and for scanning electron microscopy were prepared simultaneously. By scanning electron microscopic observation, three-dimensional information about internal structures was obtained. In the cytological analysis of the yeasts, intracellular structures were well preserved by using the freeze-substitution fixation method. On the outer leaflet of the nuclear envelope, many ribosomes were attached. The rough endoplasmic reticulum and Golgi apparatus were clearly seen in the yeast cytoplasm. The Golgi stack appeared to consist of smooth membranes, and small vesicles were present beside it. The details of other structures such as the nuclear division apparatus, actinlike filaments, and viruslike particles were also revealed. The present technique can be applied to most species of veast cells. With this new information, the previous model of a yeast cell was modified.

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Three-dimensional structure of the crystalloid in the microbody of Kloeckera sp.: composite crystal model

Cited by 10 publications

References 19 publications

Alcohol oxidase: A complex peroxisomal, oligomeric flavoprotein

Alcohol oxidase: A complex peroxisomal, oligomeric flavoprotein

Subcellular fractionation of a hypercellulolytic mutant, Trichoderma reesei Rut-C30: localization of endoglucanase in microsomal fraction

Transmission and scanning electron microscopic examination of intracellular organelles in freeze‐substituted Kloeckera and Saccharomyces cerevisiae Yeast Cells

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