• Title/Summary/Keyword: ER-mitochondria contact

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Mitochondrial Fission: Regulation and ER Connection

  • Lee, Hakjoo;Yoon, Yisang
    • Molecules and Cells
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    • v.37 no.2
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    • pp.89-94
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    • 2014
  • Fission and fusion of mitochondrial tubules are the main processes determining mitochondrial shape and size in cells. As more evidence is found for the involvement of mitochondrial morphology in human pathology, it is important to elucidate the mechanisms of mitochondrial fission and fusion. Mitochondrial morphology is highly sensitive to changing environmental conditions, indicating the involvement of cellular signaling pathways. In addition, the well-established structural connection between the endoplasmic reticulum (ER) and mitochondria has recently been found to play a role in mitochondrial fission. This minireview describes the latest advancements in understanding the regulatory mechanisms controlling mitochondrial morphology, as well as the ER-mediated structural maintenance of mitochondria, with a specific emphasis on mitochondrial fission.

Crystallization and X-ray crystallographic analysis of the PH-like domain of lipid transfer protein anchored at membrane contact sites from Saccharomyces cerevisiae

  • Tong, Junsen;Im, Young Jun
    • Biodesign
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    • v.5 no.4
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    • pp.136-140
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    • 2017
  • Lam6 is a member of sterol-specific ${\underline{l}ipid$ transfer proteins ${\underline{a}}nchored$ at ${\underline{m}ebrane$ contact sites (LAMs). Lam6 localizes to the ER-mitochondria contact sites by its PH-like domain and the C-terminal transmembrane helix. Here, we purified and crystallized the Lam6 PH-like domain from Saccharomyces cerevisiae. To aid crystallization of the Lam6 PH-like domain, T4 lysozyme was fused to the N-terminus of the Lam6 PH-like domain with a short dipeptide linker, GlySer. The fusion protein was crystallized under the condition of 0.1 M HEPES-HCl pH 7.0, 10% (w/v) PEG 8000, and 0.1 M $Na_3$ Citrate at 293K. X-ray diffraction data of the crystals were collected to $2.4{\AA}$ resolution using synchrotron radiation. The crystals belong to the orthorhombic space group $P2_12_12_1$ with unit cell parameters $a=59.5{\AA}$, $b=60.1{\AA}$, and $c=105.6{\AA}$. The asymmetric unit contains one T4L-Lam6 molecule with a solvent content of 58.7%. The initial attempt to solve the structure by molecular replacement using the T4 lysozyme structure was successful.

Light and Electron Microscopic Observations on Erythrolobus coxiae gen.et sp.nov. (Porphyridiophyceae, Rhodophyta) from Texas U.S.A.

  • Scott , Joseph L.;Baca, Bart;Ott, Franklyn D.;West, John A.
    • ALGAE
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    • v.21 no.4
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    • pp.407-416
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    • 2006
  • Low molecular weight carbohydrates, phycobilin pigments and cell structure using light and transmission electron microscopy were used to describe a new genus of unicellular red algae, Erythrolobus coxiae (Porphyridiales, Porphyrideophyceae, Rhodophyta). The nucleus of Erythrolobus is located at the cell periphery and the pyrenoid, enclosed by a cytoplasmic starch sheath, is in the cell center. The pyrenoid matrix contains branched tubular thylakoids and four or more chloroplast lobes extend from the pyrenoid along the cell periphery. A peripheral encircling thylakoid is absent. The Golgi apparatus faces outward at the cell periphery and is always associated with a mitochondrion. Porphyridium and Flintiella, the other members of the Porphyrideophyceae, also lack a peripheral encircling thylakoid and have an ER-mitochondria-Golgi association. The low molecular weight carbohydrates digeneaside and floridoside are present, unlike both Porphyridium and Flintiella, which have only floridoside. The phycobilin pigments B-phycoerythrin, R-phycocyanin and allophycocyanin are present, similar to Porphyridium purpureum. The cells have a slow gliding motility without changing shape and do not require substrate contact. The ultrastructural features are unique to members of the Porphyrideophyceae and recent molecular analyses clearly establish the validity of this new red algal class and the genus Erythrolobus.

Development of the Glandular Trichomes in Trapping Leaves of Drosera Species (끈끈이주걱속 점착식 포충엽의 분비모 발달)

  • Lee, Hye-Jin;Kim, In-Sun
    • Applied Microscopy
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    • v.39 no.1
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    • pp.57-64
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    • 2009
  • The trapping leaves of Drosera capture insects by secreting sticky mucilage from numerous glandular trichomes (GTs) that are developed on the leaf epidermis. The present study examines and compares the structural features of those trichomes in Drosera binata and D. pygmy with the use of light and electron microscopy. The study focuses primarily on the development and differentiation pattern of the GTs during growth. Upon examination, the upper and lower epidermis were readily distinguishable by the features of GTs in developing leaves. In particular, the GTs were dense in the upper epidermis and along the leaf margin. In D. binata, the capitate GTs with elongated stalk and sessile peltate GTs were found most commonly, whereas only capitate GTs with varying degrees of the stalk length were observed in D. pygmy. Up to ca. $2.2{\sim}3.4\;mm$ long capitate GTs were seen in the leaf margins of D. binata and ca. $3.7{\sim}4.2\;mm$ long GTs having racket-like head with adaxial hemispheric structures, otherwise known as tentacles, were noted in the leaf margin of D. pygmy. The peltate GTs were found to be distributed in the lower epidermis of D. binata. In both species, head cells were dense with cytoplasm containing high numbers of Golgi bodies, ER, mitochondria and small vesicles. Secretory materials accumulated within numerous small vacuoles, then fused together to form a single large vacuole, which serves as a secretory cavity. Flection movement of the marginal GTs and leaf blade GTs, and increased mucilage secretion from the head cells upon contact with prey during the capturing process are considered to be major factors in their active insectivorous mechanism. The findings of this study will be useful in comparisons to similar findings in other species that form adhesive trapping leaves, such as Drosophyllum or Pinguicula., further contributing a better understanding of the function and structure of the trapping leaves of carnivorous plants.