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Journal articles on the topic 'Microbodies'

Author: Grafiati

Published: 4 June 2021

Last updated: 29 July 2024

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1

Titus, D. E., and W. M. Becker. "Investigation of the glyoxysome-peroxisome transition in germinating cucumber cotyledons using double-label immunoelectron microscopy." Journal of Cell Biology 101, no. 4 (October 1, 1985): 1288–99. http://dx.doi.org/10.1083/jcb.101.4.1288.

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Microbodies in the cotyledons of cucumber seedlings perform two successive metabolic functions during early postgerminative development. During the first 4 or 5 d, glyoxylate cycle enzymes accumulate in microbodies called glyoxysomes. Beginning at about day 3, light-induced activities of enzymes involved in photorespiratory glycolate metabolism accumulate rapidly in microbodies. As the cotyledonary microbodies undergo a functional transition from glyoxysomal to peroxisomal metabolism, both sets of enzymes are present at the same time, either within two distinct populations of microbodies with different functions or within a single population of microbodies with a dual function. We have used protein A-gold immunoelectron microscopy to detect two glyoxylate cycle enzymes, isocitrate lyase (ICL) and malate synthase, and two glycolate pathway enzymes, serine:glyoxylate aminotransferase (SGAT) and hydroxypyruvate reductase, in microbodies of transition-stage (day 4) cotyledons. Double-label immunoelectron microscopy was used to demonstrate directly the co-existence of ICL and SGAT within individual microbodies, thereby discrediting the two-population hypothesis. Quantitation of protein A-gold labeling density confirmed that labeling was specific for microbodies. Quantitation of immunolabeling for ICL or SGAT in microbodies adjacent to lipid bodies, to chloroplasts, or to both organelles revealed very similar labeling densities in these three categories, suggesting that concentrations of glyoxysomal and peroxisomal enzymes in transition-stage microbodies probably cannot be predicted based on the apparent associations of microbodies with other organelles.

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2

Kim, Ki Woo, Eun Woo Park, and Kyung Soo Kim. "Glyoxysomal Nature of Microbodies Complexed with Lipid Globules in Botryosphaeria dothidea." Phytopathology® 94, no. 9 (September 2004): 970–77. http://dx.doi.org/10.1094/phyto.2004.94.9.970.

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The glyoxysomal nature of microbodies was determined in Botryosphaeria dothidea hyphae based on morphology and in situ enzyme characteristics by transmission electron microscopy and cytochemistry. Bound by a single membrane, microbodies had a homogeneous matrix and varied in size ranging from 200 to 400 nm in diameter. Microbodies often had crystalline inclusions that consisted of parallel arrays of fine tubules in their matrices. Microbodies and lipid globules were placed in close association with each other, forming microbody-lipid globule complexes in hyphae. The cytochemical activities of catalase and malate synthase were localized in microbodies, showing intense electron density of the organelle. In addition, immunogold labeling detected the presence of catalase in a multivesicular body-like organelle and the cell wall as well as in the matrix and crystalline inclusion of microbodies, supporting the enzyme secretion outward. Meanwhile, isocitrate lyase was localized only in matrices of microbodies. These results suggest that the microbodies complexed with lipid globules in B. dothidea hyphae are functionally defined as glyoxysomes which may enable the fungus to survive latent periods using lipids via the glyoxylate cycle and catalase secretion.

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3

Carson, David B., and Joseph J. Cooney. "Characterization of partially purified microbodies from hydrocarbon-grown cells of Cladosporium resinae." Canadian Journal of Microbiology 35, no. 5 (May 1, 1989): 565–72. http://dx.doi.org/10.1139/m89-090.

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Cells of the filamentous fungus Cladosporium resinae synthesize many more microbodies when they are grown on an n-alkane than when they are grown on glucose. Cladosporium resinae was grown on n-dodecane and spheroplasts were prepared, disrupted, and fractionated by differential and density gradient centrifugation. A fraction was isolated which was enriched in catalase, a marker enzyme for microbodies. Another fraction was isolated which was enriched in cytochrome c oxidase, a marker for mitochondria. Urate oxidase, a second marker for microbodies, was not detected in cell extracts. The microbody and mitochondrial fractions were relatively free of contamination from the endoplasmic reticulum and cytosol as indicated by the amounts of glucose-6-phosphatase and glucose-6-phosphate dehydrogenase present, respectively. Transmission electron microscopy revealed that the catalase-enriched fraction contained intact microbodies, with mitochondria as a minor contaminant. Catalase was localized in microbodies by staining with 3,3′-diaminobenzidine. Mitochrondria were present in the cytochrome c oxidase enriched fraction and took up the vital stain Janus green B. In similar preparations from cells grown on glucose, catalase was largely nonparticulate. Microbodies were not observed in thin sections prepared from density gradient fractions, but mitochondria were present in a cytochrome c oxidase enriched fraction.Key words: Cladosporium resinae, microbodies, mitochondria, catalase, cytochrome c oxidase.

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4

Schliebs, Wolfgang, Christian Würtz, Wolf-Hubert Kunau, Marten Veenhuis, and Hanspeter Rottensteiner. "A Eukaryote without Catalase-Containing Microbodies: Neurospora crassa Exhibits a Unique Cellular Distribution of Its Four Catalases." Eukaryotic Cell 5, no. 9 (September 2006): 1490–502. http://dx.doi.org/10.1128/ec.00113-06.

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ABSTRACT Microbodies usually house catalase to decompose hydrogen peroxide generated within the organelle by the action of various oxidases. Here we have analyzed whether peroxisomes (i.e., catalase-containing microbodies) exist in Neurospora crassa. Three distinct catalase isoforms were identified by native catalase activity gels under various peroxisome-inducing conditions. Subcellular fractionation by density gradient centrifugation revealed that most of the spectrophotometrically measured activity was present in the light upper fractions, with an additional small peak coinciding with the peak fractions of HEX-1, the marker protein for Woronin bodies, a compartment related to the microbody family. However, neither in-gel assays nor monospecific antibodies generated against the three purified catalases detected the enzymes in any dense organellar fraction. Furthermore, staining of an N. crassa wild-type strain with 3,3′-diaminobenzidine and H2O2 did not lead to catalase-dependent reaction products within microbodies. Nonetheless, N. crassa does possess a gene (cat-4) whose product is most similar to the peroxisomal type of monofunctional catalases. This novel protein indeed exhibited catalase activity, but was not localized to microbodies either. We conclude that N. crassa lacks catalase-containing peroxisomes, a characteristic that is probably restricted to a few filamentous fungi that produce little hydrogen peroxide within microbodies.

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5

Carson, David B., and Joseph J. Cooney. "Microbodies in fungi: a review." Journal of Industrial Microbiology 6, no. 1 (September 1990): 1–18. http://dx.doi.org/10.1007/bf01576172.

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6

Stabenau, Helmut, Werner Säftel, and Uwe Winkler. "Microbodies of the alga Chara." Physiologia Plantarum 118, no. 1 (April 16, 2003): 16–20. http://dx.doi.org/10.1034/j.1399-3054.2003.00004.x.

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7

Hajra, A. "Glycerolipid biosynthesis in peroxisomes (microbodies)." Progress in Lipid Research 34, no. 4 (December 1995): 343–64. http://dx.doi.org/10.1016/0163-7827(95)00013-5.

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8

Veenhuis, M., M. Mateblowski, W. H. Kunau, and W. Harder. "Proliferation of microbodies inSaccharomyces cerevisiae." Yeast 3, no. 2 (June 1987): 77–84. http://dx.doi.org/10.1002/yea.320030204.

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9

Pan, Yanhong, Wenxia Zheng, Alison E. Moyer, Jingmai K. O’Connor, Min Wang, Xiaoting Zheng, Xiaoli Wang, Elena R. Schroeter, Zhonghe Zhou, and Mary H. Schweitzer. "Molecular evidence of keratin and melanosomes in feathers of the Early Cretaceous bird Eoconfuciusornis." Proceedings of the National Academy of Sciences 113, no. 49 (November 21, 2016): E7900—E7907. http://dx.doi.org/10.1073/pnas.1617168113.

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Microbodies associated with feathers of both nonavian dinosaurs and early birds were first identified as bacteria but have been reinterpreted as melanosomes. Whereas melanosomes in modern feathers are always surrounded by and embedded in keratin, melanosomes embedded in keratin in fossils has not been demonstrated. Here we provide multiple independent molecular analyses of both microbodies and the associated matrix recovered from feathers of a new specimen of the basal bird Eoconfuciusornis from the Early Cretaceous Jehol Biota of China. Our work represents the oldest ultrastructural and immunological recognition of avian beta-keratin from an Early Cretaceous (∼130-Ma) bird. We apply immunogold to identify protein epitopes at high resolution, by localizing antibody–antigen complexes to specific fossil ultrastructures. Retention of original keratinous proteins in the matrix surrounding electron-opaque microbodies supports their assignment as melanosomes and adds to the criteria employable to distinguish melanosomes from microbial bodies. Our work sheds new light on molecular preservation within normally labile tissues preserved in fossils.

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10

Keller, G. A., S. Krisans, S. J. Gould, J. M. Sommer, C. C. Wang, W. Schliebs, W. Kunau, S. Brody, and S. Subramani. "Evolutionary conservation of a microbody targeting signal that targets proteins to peroxisomes, glyoxysomes, and glycosomes." Journal of Cell Biology 114, no. 5 (September 1, 1991): 893–904. http://dx.doi.org/10.1083/jcb.114.5.893.

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Peroxisomes, glyoxysomes, glycosomes, and hydrogenosomes have each been classified as microbodies, i.e., subcellular organelles with an electron-dense matrix that is bound by a single membrane. We investigated whether these organelles might share a common evolutionary origin by asking if targeting signals used for translocation of proteins into these microbodies are related. A peroxisomal targeting signal (PTS) consisting of the COOH-terminal tripeptide serine-lysine-leucine-COOH has been identified in a number of peroxisomal proteins (Gould, S.J., G.-A. Keller, N. Hosken, J. Wilkinson, and S. Subramani. 1989. J. Cell Biol. 108:1657-1664). Antibodies raised to a peptide ending in this sequence (SKL-COOH) recognize a number of peroxisomal proteins. Immunocryoelectron microscopy experiments using this anti-SKL antibody revealed the presence of proteins containing the PTS within glyoxysomes of cells from Pichia pastoris, germinating castor bean seeds, and Neurospora crassa, as well as within the glycosomes of Trypanosoma brucei. Western blot analysis of purified organelle fractions revealed the presence of many proteins containing this PTS in both glyoxysomes and glycosomes. These results indicate that at least one of the signals, and therefore the mechanism, for protein translocation into peroxisomes, glyoxysomes, and glycosomes has been conserved, lending support to a common evolutionary origin for these microbodies. Hydrogenosomes, the fourth type of microbody, did not contain proteins that cross-reacted with the anti-PTS antibody, suggesting that this organelle is unrelated to microbodies.

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11

Werner, Antonia, Kolja Otte, Gertrud Stahlhut, Leon M. Hanke, and Stefanie Pöggeler. "The Glyoxysomal Protease LON2 Is Involved in Fruiting-Body Development, Ascosporogenesis and Stress Resistance in Sordaria macrospora." Journal of Fungi 7, no. 2 (January 26, 2021): 82. http://dx.doi.org/10.3390/jof7020082.

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Microbodies, including peroxisomes, glyoxysomes and Woronin bodies, are ubiquitous dynamic organelles that play important roles in fungal development. The ATP-dependent chaperone and protease family Lon that maintain protein quality control within the organelle significantly regulate the functionality of microbodies. The filamentous ascomycete Sordaria macrospora is a model organism for studying fruiting-body development. The genome of S. macrospora encodes one Lon protease with the C-terminal peroxisomal targeting signal (PTS1) serine-arginine-leucine (SRL) for import into microbodies. Here, we investigated the function of the protease SmLON2 in sexual development and during growth under stress conditions. Localization studies revealed a predominant localization of SmLON2 in glyoxysomes. This localization depends on PTS1, since a variant without the C-terminal SRL motif was localized in the cytoplasm. A ΔSmlon2 mutant displayed a massive production of aerial hyphae, and produced a reduced number of fruiting bodies and ascospores. In addition, the growth of the ΔSmlon2 mutant was completely blocked under mild oxidative stress conditions. Most of the defects could be complemented with both variants of SmLON2, with and without PTS1, suggesting a dual function of SmLON2, not only in microbody, but also in cytosolic protein quality control.

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12

Hayashi, Yasuko, and Akiko Shinozaki. "Visualization of microbodies in Chlamydomonas reinhardtii." Journal of Plant Research 125, no. 4 (December 29, 2011): 579–86. http://dx.doi.org/10.1007/s10265-011-0469-z.

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13

Müller, Wally H., Roelof A. L. Bovenberg, Marloes H. Groothuis, Fred Kattevilder, Erik B. Smaal, Lucia H. M. Van der Voort, and Arie J. Verkleij. "Involvement of microbodies in penicillin biosynthesis." Biochimica et Biophysica Acta (BBA) - General Subjects 1116, no. 2 (April 1992): 210–13. http://dx.doi.org/10.1016/0304-4165(92)90118-e.

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14

Landolt, Reto, and Philippe Matile. "Glyoxisome-like microbodies in senescent spinach leaves." Plant Science 72, no. 2 (January 1990): 159–63. http://dx.doi.org/10.1016/0168-9452(90)90078-3.

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15

Guerra-Giraldez, Cristina, Luis Quijada, and Christine E. Clayton. "Compartmentation of enzymes in a microbody, the glycosome, is essential in Trypanosoma brucei." Journal of Cell Science 115, no. 13 (July 1, 2002): 2651–58. http://dx.doi.org/10.1242/jcs.115.13.2651.

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All kinetoplastids contain membrane-bound microbodies known as glycosomes,in which several metabolic pathways including part of glycolysis are compartmentalized. Peroxin 2 is essential for the import of many proteins into the microbodies of yeasts and mammals. The PEX2 gene of Trypanosoma brucei was identified and its expression was silenced by means of tetracycline-inducible RNA interference. Bloodstream-form trypanosomes, which rely exclusively on glycolysis for ATP generation, died rapidly upon PEX2 depletion. Insect-form (procyclic) trypanosomes do not rely solely on glycolysis for ATP synthesis. PEX2 depletion in procyclic forms resulted in relocation of most tested matrix proteins to the cytosol, and these mutants also died. Compartmentation of microbody enzymes is therefore essential for survival of bloodstream and procyclic T. brucei. In contrast, yeasts and cultured mammalian cells grow normally in the absence of peroxisomal membranes unless placed on selective media.

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16

Nishimura, Mikio, Makoto Hayashi, Akira Kato, Katsushi Yamaguchi, and Shoji Mano. "Functional Transformation of Microbodies in Higher Plant Cells." Cell Structure and Function 21, no. 5 (1996): 387–93. http://dx.doi.org/10.1247/csf.21.387.

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17

Nishizawa, Naoko-Kishi, and Satoshi Mori. "Microbodies containing crystalloid inclusions in rice root cells." Soil Science and Plant Nutrition 35, no. 3 (September 1989): 485–90. http://dx.doi.org/10.1080/00380768.1989.10434782.

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18

SAUTTER, C. "Immunolocalization studies in the biogenesis of plant microbodies." Cell Biology International Reports 13, no. 1 (January 1989): 65–72. http://dx.doi.org/10.1016/s0309-1651(89)80008-6.

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19

de Hoop, M. J., and G. Ab. "Import of proteins into peroxisomes and other microbodies." Biochemical Journal 286, no. 3 (September 15, 1992): 657–69. http://dx.doi.org/10.1042/bj2860657.

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20

Veenhuis, Marten, Grietje Sulter, Ida van der Klei, and Wim Harder. "Evidence for functional heterogeneity among microbodies in yeasts." Archives of Microbiology 151, no. 2 (January 1989): 105–10. http://dx.doi.org/10.1007/bf00414422.

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21

Borst, Piet. "How proteins get into microbodies (peroxisomes, glyoxysomes, glycosomes)." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 866, no. 4 (May 1986): 179–203. http://dx.doi.org/10.1016/0167-4781(86)90044-8.

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22

Lindgren, Johan, Alison Moyer, Mary H. Schweitzer, Peter Sjövall, Per Uvdal, Dan E. Nilsson, Jimmy Heimdal, et al. "Interpreting melanin-based coloration through deep time: a critical review." Proceedings of the Royal Society B: Biological Sciences 282, no. 1813 (August 22, 2015): 20150614. http://dx.doi.org/10.1098/rspb.2015.0614.

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Colour, derived primarily from melanin and/or carotenoid pigments, is integral to many aspects of behaviour in living vertebrates, including social signalling, sexual display and crypsis. Thus, identifying biochromes in extinct animals can shed light on the acquisition and evolution of these biological traits. Both eumelanin and melanin-containing cellular organelles (melanosomes) are preserved in fossils, but recognizing traces of ancient melanin-based coloration is fraught with interpretative ambiguity, especially when observations are based on morphological evidence alone. Assigning microbodies (or, more often reported, their ‘mouldic impressions’) as melanosome traces without adequately excluding a bacterial origin is also problematic because microbes are pervasive and intimately involved in organismal degradation. Additionally, some forms synthesize melanin. In this review, we survey both vertebrate and microbial melanization, and explore the conflicts influencing assessment of microbodies preserved in association with ancient animal soft tissues. We discuss the types of data used to interpret fossil melanosomes and evaluate whether these are sufficient for definitive diagnosis. Finally, we outline an integrated morphological and geochemical approach for detecting endogenous pigment remains and associated microstructures in multimillion-year-old fossils.

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23

Courtois-Verniquet, F., and R. Douce. "Lack of aconitase in glyoxysomes and peroxisomes." Biochemical Journal 294, no. 1 (August 15, 1993): 103–7. http://dx.doi.org/10.1042/bj2940103.

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The aim of this work was to find out whether aconitase [citrate (isocitrate) hydro-lyase, EC 4.2.1.3] which is rapidly inactivated by H2O2, is present in the microbodies from plant cells. The separation of intact organelles from castor-bean (Ricinus communis) endosperm and potato (Solanum tuberosum) tuber indicated that aconitase activity is essentially limited to the mitochondria and cytosol fraction, but was not detected in highly purified castor-bean endosperm and potato tuber peroxisomes. An isotropic e.p.r. signal of the type expected for the 3Fe cluster of oxidized aconitase was not detected in microbodies. In immunoblot analyses, antibodies raised against potato tuber mitochondrial aconitase did not cross-react with any glyoxysomal or peroxisomal protein. Positive reactions were found for cytosol fraction and mitochondria of castor-bean endosperm. The operation of the full glyoxylate cycle in isolated glyoxysomes requires the presence of aconitase in the incubation medium. It is concluded that glyoxysomes are probably devoid of aconitase and that the glyoxylate cycle requires a detour via the cytosol, which contains a powerful aconitase activity.

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24

CAVALIER-SMITH, T. "The Simultaneous Symbiotic Origin of Mitochondria, Chloroplasts, and Microbodies." Annals of the New York Academy of Sciences 503, no. 1 Endocytobiolo (July 1987): 55–71. http://dx.doi.org/10.1111/j.1749-6632.1987.tb40597.x.

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25

Nolan, Richard A., Christopher J. Clovis, and William S. Davidson. "Microbodies and a virus-like particle in Entomophaga aulicae." Transactions of the British Mycological Society 90, no. 2 (March 1988): 315–18. http://dx.doi.org/10.1016/s0007-1536(88)80103-7.

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26

Murrin, F., W. Newcomb, and I. B. Heath. "Ultrastructure of Microbodies in Protoplasts and Hyphae ofEntomophaga Aulicae(Zygomycetes)." Mycologia 79, no. 4 (July 1987): 559–64. http://dx.doi.org/10.1080/00275514.1987.12025424.

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27

Veenhuis, M., M. C. Hoogkamer-Te Niet, and W. J. Middelhoven. "Biogenesis and metabolic significance of microbodies in urate-utilizing yeasts." Antonie van Leeuwenhoek 51, no. 1 (1985): 33–43. http://dx.doi.org/10.1007/bf00444226.

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28

Dijksterhuis, Jan, and Marten Veenhuis. "Development and metabolic significance of microbodies in the nematophagous fungus." Ultramicroscopy 31, no. 4 (December 1989): 462. http://dx.doi.org/10.1016/0304-3991(89)90357-4.

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29

Sakajo, Shigeru, and Tadashi Asahi. "In vitro synthesis of catalase protein in sweet potato root microbodies." FEBS Letters 205, no. 2 (September 15, 1986): 337–40. http://dx.doi.org/10.1016/0014-5793(86)80924-3.

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30

Murrin, F., W. Newcomb, and I. B. Heath. "Ultrastructure of Microbodies in Protoplasts and Hyphae of Entomophaga aulicae (Zygomycetes)." Mycologia 79, no. 4 (July 1987): 559. http://dx.doi.org/10.2307/3807595.

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31

Clayton, C. E. "Import of fructose bisphosphate aldolase into the glycosomes of Trypanosoma brucei." Journal of Cell Biology 105, no. 6 (December 1, 1987): 2649–54. http://dx.doi.org/10.1083/jcb.105.6.2649.

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The glycolytic enzymes of Trypanosomatids are compartmentalized within peroxisome-like microbodies called glycosomes. Fructose bisphosphate aldolase is synthesized on free polysomes and imported into glycosomes within 5 min. Peptide mapping reveals no primary structural differences between the in vivo-synthesized protein and that made in vitro from a synthetic template. However, native aldolase from glycosomes is partially protease resistant, whereas the in vitro translation product is not. Pulse-chase results indicate that aldolase in bloodstream trypanosomes has a much longer half-life than in the procyclic tsetse fly form.

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32

Veenhuis, M., and J. M. Goodman. "Peroxisomal assembly: membrane proliferation precedes the induction of the abundant matrix proteins in the methylotrophic yeast Candida boidinii." Journal of Cell Science 96, no. 4 (August 1, 1990): 583–90. http://dx.doi.org/10.1242/jcs.96.4.583.

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Peroxisomes are massively induced when methylotrophic yeasts are cultured in medium containing methanol. These organelles contain enzymes that catalyze the initial steps of methanol assimilation. In Candida boidinii, a methylotrophic yeast, the peroxisomal matrix (internal compartment) is composed almost exclusively of two proteins, alcohol oxidase and dihydroxyacetone synthase; catalase is present in much lower abundance. Monoclonal and polyclonal antibodies are available against peroxisomal matrix and membrane proteins. These were utilized to correlate the induction of specific proteins with the morphological changes occurring during peroxisomal proliferation. Cells cultured in glucose-containing medium contain two to five small microbodies, which are identifiable by catalase staining and immunoreactivity with a monoclonal antibody against PMP47, an integral peroxisomal membrane protein. Three stages of proliferation can be distinguished when cells are switched to methanol as the carbon source. (1) There is an early stage (within 1 h) in which several peroxisomes develop from a preexisting organelle. This is accompanied by an increase in catalase activity and an induction of PMP47, but no detectable induction of alcohol oxidase or dihydroxyacetone synthase is observed. (2) From 1 to 2.5 h there is further division of these microbodies until up to 30 small peroxisomes generally are present in each of one or two clusters per cell. Induction of alcohol oxidase, dihydroxyacetone synthase and PMP20, a protein that is distributed in the matrix and membrane, is detectable during this time. Serial sections reveal that some peroxisomes remain uninduced while others undergo proliferation. Such sections also show no obvious connections between peroxisomes within clusters.(ABSTRACT TRUNCATED AT 250 WORDS)

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33

Teijeira, Fernando, Ricardo V. Ullán, Susana M. Guerra, Carlos García-Estrada, Inmaculada Vaca, and Juan F. Martín. "The transporter CefM involved in translocation of biosynthetic intermediates is essential for cephalosporin production." Biochemical Journal 418, no. 1 (January 28, 2009): 113–24. http://dx.doi.org/10.1042/bj20081180.

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The cluster of early cephalosporin biosynthesis genes (pcbAB, pcbC, cefD1, cefD2 and cefT of Acremonium chrysogenum) contains all of the genes required for the biosynthesis of the cephalosporin biosynthetic pathway intermediate penicillin N. Downstream of the cefD1 gene, there is an unassigned open reading frame named cefM encoding a protein of the MFS (major facilitator superfamily) with 12 transmembrane domains, different from the previously reported cefT. Targeted inactivation of cefM by gene replacement showed that it is essential for cephalosporin biosynthesis. The disrupted mutant accumulates a significant amount of penicillin N, is unable to synthesize deacetoxy-, deacetyl-cephalosporin C and cephalosporin C and shows impaired differentiation into arthrospores. Complementation of the disrupted mutant with the cefM gene restored the intracellular penicillin N concentration to normal levels and allowed synthesis and secretion of the cephalosporin intermediates and cephalosporin C. A fused cefM-gfp gene complemented the cefM-disrupted mutant, and the CefM–GFP (green fluorescent protein) fusion was targeted to intracellular microbodies that were abundant after 72 h of culture in the differentiating hyphae and in the arthrospore chains, coinciding with the phase of intense cephalosporin biosynthesis. Since the dual-component enzyme system CefD1–CefD2 that converts isopenicillin N into penicillin N contains peroxisomal targeting sequences, it is probable that the epimerization step takes place in the peroxisome matrix. The CefM protein seems to be involved in the translocation of penicillin N from the peroxisome (or peroxisome-like microbodies) lumen to the cytosol, where it is converted into cephalosporin C.

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34

Fiedler, S., Th Schnelle, B. Wagner, and G. Fuhr. "Electrocasting - formation and structuring of suspended microbodies using a.c. generated field cages." Microsystem Technologies 2, no. 1 (March 1995): 1–7. http://dx.doi.org/10.1007/bf02739520.

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35

Opperdoes, Fred R., Eva Nohynkova, Emile Van Schaftingen, Anne-Marie Lambeir, Marten Veenhuis, and Joris Van Roy. "Demonstration of glycosomes (microbodies) in the bodonid flagellate Trypanoplasma borelli (protozoa, kinetoplastida)." Molecular and Biochemical Parasitology 30, no. 2 (August 1988): 155–63. http://dx.doi.org/10.1016/0166-6851(88)90108-9.

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36

Burgess, N., G. W. Beakes, and D. R. Thomas. "Separation of mitochondria from microbodies of Pisum sativum (L. cv. Alaska) cotyledons." Planta 166, no. 2 (October 1985): 151–55. http://dx.doi.org/10.1007/bf00397341.

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37

Ding, M., C. Clayton, and D. Soldati. "Toxoplasma gondii catalase: are there peroxisomes in toxoplasma?" Journal of Cell Science 113, no. 13 (July 1, 2000): 2409–19. http://dx.doi.org/10.1242/jcs.113.13.2409.

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The intracellular protozoan parasite Toxoplasma gondii, like all members of the phylum Apicomplexa, is known to possess many organelles: in addition to mitochondria and the compartments of the secretory pathway, there is a reduced chloroplast (the apicoplast) and the phylum-specific components of the apical complex: dense granules, micronemes and rhoptries. Conspicuously missing so far are microbodies, organelles that can be found in nearly all eukaryotic organisms. Microbodies show a large variation with regard to their size, number and contents, depending on the organism and cell type. One marker enzyme of this single membrane-bound organelle is catalase, which is responsible for the degradation of hydrogen peroxide to water and oxygen. The EST project in T. gondii revealed the existence of two overlapping clones which showed similarity with catalase, and these were used to clone the corresponding gene. The predicted sequence of T. gondii catalase has -AKM at the C terminus, which falls within the consensus of the PTS1 peroxisomal targeting signal. Southern blot analysis confirmed the presence of a single copy gene. Northern and western blot analyses showed that the catalase gene is transcribed and translated. Immunofluorescence assays using an antibody raised against a catalase peptide identified a distinct structure towards the apical end, but other catalase-specific antibodies failed to confirm this localisation. Cell fractionations indicated that the majority of the enzyme was in the cytosol. The fusion of the C-terminal twelve amino acids, including AKM, or the canonical peroxisomal targeting signal, -SKL, to GFP resulted in predominantly cytosolic localization in T. gondii. There was therefore no evidence for membrane-bound peroxisomes in Toxoplasma.

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38

Mori, Hitoshi, and Mikio Nishimura. "Glyoxysomal malate synthetase is specifically degraded in microbodies during greening of pumpkin cotyledons." FEBS Letters 244, no. 1 (February 13, 1989): 163–66. http://dx.doi.org/10.1016/0014-5793(89)81184-6.

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Carson, David B., and Joseph J. Cooney. "Spheroplast formation and partial purification of microbodies from hydrocarbon-grown cells ofCladosporium resinae." Journal of Industrial Microbiology 3, no. 2 (April 1988): 111–17. http://dx.doi.org/10.1007/bf01569552.

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40

Charzynska, Maria, Meri Murgia, and M. Cresti. "Ultrastructure of the vegetative cell ofBrassica napus pollen with particular reference to microbodies." Protoplasma 152, no. 1 (February 1989): 22–28. http://dx.doi.org/10.1007/bf01354236.

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McLaughlin, David J., Gail J. Celio, Mahajabeen Padamsee, and Bryn T. M. Dentinger. "Cystidial structure in two genera of the Russulales." Botany 86, no. 6 (June 2008): 545–50. http://dx.doi.org/10.1139/b08-021.

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As a part of a broader study to determine whether the subcellular structure of cystidia can provide synapomorphies for clades of Agaricomycetes, cystidia of Auriscalpium vulgare Gray and Russula emetica (Schaeff.) Pers. were examined ultrastructurally, after freeze substitution. Vesicles with tubular invaginations occurred in immature hymenial cystidia of both species, and microbodies were also present. Gloeohyphae of A. vulgare also contained these organelles. The tubular invaginations disappeared from the vesicles in maturing cystidia of A. vulgare and were replaced by electron-dense deposits. These patterns of cellular organization may be synapomorphic for the Russulales. The data will be incorporated into the “Assembling the Fungal Tree of Life” (AFTOL) Structural and Biochemical Database to facilitate the use of morphological characters in phylogenetic analyses.

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42

Hayashi, Makoto, Masahiro Aoki, Akira Kato, Maki Kondo, and Mikio Nishimura. "Transport of chimeric proteins that contain a carboxy-terminal targeting signal into plant microbodies." Plant Journal 10, no. 2 (August 1996): 225–34. http://dx.doi.org/10.1046/j.1365-313x.1996.10020225.x.

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Klinger, Michael, Christopher Laske, Mario Graeve, Martin Thoma, and Andreas Traube. "A Sensor for the In-Flight Detection of Single Fluorescent Microbodies in Nanoliter Droplets." IEEE Sensors Journal 20, no. 11 (June 1, 2020): 5809–17. http://dx.doi.org/10.1109/jsen.2020.2972268.

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Mano, S., M. Hayashi, M. Kondo, and M. Nishimura. "Hydroxypyruvate Reductase with a Carboxy-Terminal Targeting Signal to Microbodies is Expressed in Arabidopsis." Plant and Cell Physiology 38, no. 4 (January 1, 1997): 449–55. http://dx.doi.org/10.1093/oxfordjournals.pcp.a029188.

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Ivanova, S. V., S. Ya Betsofen, A. A. Lozovan, D. E. Molostov, and M. I. Pikus. "Structure of the surface layers on zirconium products after dynamic impact of the microbodies." Journal of Physics: Conference Series 872 (July 2017): 012039. http://dx.doi.org/10.1088/1742-6596/872/1/012039.

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Ye, Min, Meizhao Le, Yuanmin Li, Xiaoming Song, and Guimei Li. "Derivative Collagen Fibers Within Microbodies and Intra-Hepatocytes Fibrosis in Three Human Choledocholithiasis Cases." Ultrastructural Pathology 26, no. 5 (January 2002): 341–43. http://dx.doi.org/10.1080/01913120290104638.

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Veenhuis, Marten, Cobie Van Wijk, Urs Wyss, Birgit Nordbring-Hertz, and Wim Harder. "Significance of electron dense microbodies in trap cells of the nematophagous fungus Arthrobotrys oligospora." Antonie van Leeuwenhoek 56, no. 3 (October 1989): 251–61. http://dx.doi.org/10.1007/bf00418937.

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Fiskin, A. M., and R. G. Garrison. "Double-membraned vesicles and their possible role in the ontogeny of microbodies of Basidiobolus haptosporus." Annales de l'Institut Pasteur / Microbiologie 137, no. 1 (January 1986): 15–31. http://dx.doi.org/10.1016/s0769-2609(86)80002-3.

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Veenhuis, Marten, Birgit Nordbring-Hertz, and Wim Harder. "Development and fate of electron-dense microbodies in trap cells of the nematophagous fungusArthrobotrys oligospora." Antonie van Leeuwenhoek 51, no. 4 (July 1985): 399–407. http://dx.doi.org/10.1007/bf02275044.

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Jimenez, Desmond R., and Martha Gilliam. "Cytochemistry of peroxisomal enzymes in microbodies of the midgut of the honey bee, Apis mellifera." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 90, no. 4 (January 1988): 757–66. http://dx.doi.org/10.1016/0305-0491(88)90331-8.

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