Two action sites of AM-toxin I produced by apple pathotype of Alternaria alternata in host cells: an ultrastructural study

1981 ◽  
Vol 59 (3) ◽  
pp. 301-310 ◽  
Author(s):  
Pyoyun Park ◽  
Syoyo Nishimura ◽  
Keisuke Kohmoto ◽  
Hiroshi Otani ◽  
Kazuyuki Tsujimoto
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Amorphous Materials ◽  
Plasma Membranes ◽  
Host Cells ◽  
Ultrastructural Changes ◽  
Electron Microscopic ◽  
Electron Microscopic Autoradiography ◽  
Moderately Resistant ◽  
Membrane Cell

The localization of primary action sites of AM-toxin I in host cells was examined by ultrastructural investigation and electron microscopic autoradiography. In susceptible apple leaves, the first effect of the toxin appeared 1 h after treatment in the plasma membranes and chloroplasts of mesophyll and vascular bundle sheath cells and in the plasma membranes of phloem and epidermal cells. Membranes and vesicles which were stained positively with a specific staining solution for grana lamellae were found in the matrix of the chloroplasts, showing that the membranous materials were derived from the disrupted grana. Cell wall lesions were formed around plasmodesmata where plasma membranes were invaginated. The invaginated sites were filled with amorphous materials from degraded cell walls, including membranes derived from plasma membranes and the desmotubules extending from plasmodesmata. The modified chloroplasts and plasma membranes were observed more often as the time after the toxin treatment was prolonged. Modified plastids were not found in the leaf cells. The other cellular membranes appeared normal even 10 h after the treatment. Resistant leaf cells were rarely affected by the toxin. Not all tissues from susceptible apples were sensitive as the toxin caused no necrosis or ultrastructural changes in petal cells. Resistant petal cells were also insensitive to the toxin, but the toxin causes necrosis and ultrastructural changes in moderately resistant petal cells in which the primary effect of the toxin appeared as plasma membrane modifications. Plastids were not affected by the toxin. These results indicate that the action sites of the toxin may be located on the plasma membrane – cell wall association in susceptible leaf cells and in moderately resistant petal cells and also on the chloroplasts of susceptible cells. The results of electron microscopic autoradiography also provided evidence that the action sites of the toxin were present on chloroplasts and the plasma membrane –cell wall association of susceptible leaf cells.

Effect of a host-specific toxin (AM-toxin I) produced by Alternaria mali, an apple pathogen, on the ultrastructure of plasma membrane of cells in apple and Japanese pear leaves

1977 ◽  
Vol 55 (18) ◽  
pp. 2383-2393 ◽  
Author(s):  
Pyoyun Park ◽  
Mitsuya Tsuda ◽  
Yoshiharu Hayashi ◽  
Tamio Ueno
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Plasma Membranes ◽  
Plant Cells ◽  
Host Cells ◽  
Japanese Pear ◽  
Susceptible Plant ◽  
Secondary Effects ◽  
Permeability Changes ◽  
Ultrastructural Modifications

AM-toxin I (4 μg/ml), a host-specific toxin of Alternaria mali, caused permeability changes in susceptible apple and Nijisseiki pear leaves within 5 min of treatment. The first effect of the toxin appeared on plasma membranes of susceptible apple cells. One hour after toxin treatment, slight invaginations were evident in plasma membranes near plasmodesmata. Six hours after treatment, the spaces between cell wall and invaginated plasma membrane contained lomasome-like vesicles, membranous fragments, and desmotubules extending from plasmodesmata. The membranous materials appeared to originate from the plasma membrane. Thirty-one hours after treatment, necrotic cells of susceptible leaves showed the general disruptions of cellular membranes which might be caused by secondary effects of the toxin. The similar changes of plasma membrane and plasmodesmata also were found in Nijisseiki pear cells treated with AM-toxin I (4 μg/ml) for 1 h and 6 h. The invaginations of the plasma membrane at plasmodesmata were the first ultrastructural modifications in the toxin-treated Nijisseiki cells. AM-toxin I did not affect the ultrastructure of resistant apple and Chojuro pear cells. These results indicate that the initial sites for the toxin may be on the plasma membrane of the susceptible apple cells. Furthermore, the results suggest that the plasma membrane modifications are associated with permeability changes in the toxin-treated, susceptible plant cells except for original host cells treated with the toxin.

Enrichment of vitronectin- and fibronectin-like proteins in NaCI-adapted plant cells and evidence for their involvement in plasma membrane-cell wall adhesion

1993 ◽  
Vol 3 (5) ◽  
pp. 637-646 ◽  
Author(s):  
Jian-Kang Zhu ◽  
Jun Shi ◽  
Utpal Singh ◽  
Sarah E. Wyatt ◽  
Ray A. Bressan ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Plant Cells ◽  
Membrane Cell

scholarly journals Formation of flavone-based wooly fibres by glandular trichomes of Dionysia tapetodes

2020 ◽  
Author(s):  
Matthieu Bourdon ◽  
Josephine Gaynord ◽  
Karin Müller ◽  
Gareth Evans ◽  
Simon Wallis ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Cell Biology ◽  
Glandular Trichomes ◽  
Thread Formation ◽  
Flavone Derivatives ◽  
Chemical Techniques ◽  
Surface Covering ◽  
Membrane Cell ◽  
Putative Mechanism

AbstractDionysia tapetodes, a small cushion-forming mountainous evergreen in the Primulaceae, possesses a vast surface-covering of long silky fibres forming the characteristic “wooly” farina. This contrasts with some related Primula which instead possess a powdery farina. Using a combination of cell biology and analytical chemical techniques, we provide a detailed insight of wooly farina formation by glandular trichomes that produce a mixture of flavone and substituted flavone derivatives, including hydroxyflavones. Conversely, our analysis show that the powdery form consist almost entirely of flavone. The wooly farina in D. tapetodes is extruded through specific sites at the surface of the glandular head cell, characterised by a small complete gap in the plasma membrane, cell wall and cuticle. The data is consistent with formation and thread elongation occurring from within the cell. The putative mechanism of wool thread formation and its stability is discussed.

The isolation of plasma membrane from protoplasts of soybean suspension cultures

1977 ◽  
Vol 24 (1) ◽  
pp. 295-310
Author(s):  
D.W. Galbraith ◽  
D.H. Northcote
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Membrane Fraction ◽  
Sucrose Gradient ◽  
Plasma Membranes ◽  
Gradient Centrifugation ◽  
Buoyant Density ◽  
Membrane Systems ◽  
Enzymic Digestion ◽  
Nadh Cytochrome

A procedure for the isolation of plasma membranes from protoplasts of suspension-cultured soybean is described. Protoplasts were prepared by enzymic digestion of the cell wall and the plasma membrane was labelled with radioactive diazotized sulphanilic acid. The membrane systems from broken protoplasts were separated by continuous isopycnic sucrose gradient centrifugation. Radioactivity was localized in a band possessing a buoyant density of 1–14 g ml-1. The activities of NADPH- and NADH-cytochrome c reductase, fumarase, Mg2+-ATPase, IDPase and acid phosphodiesterase in the various regions of the density gradient were determined. A plasma membrane fraction was selected which was relatively uncontaminated with membranes derived from endoplasmic reticulum, tonoplasts and mitochondria. The results indicated that Mg2+-ATPase and possibly acid phosphodiesterase were associated with the plasma membrane.

Ultrastructure of compatible and incompatible reactions of sunflower to Plasmopara halstedii

1979 ◽  
Vol 57 (4) ◽  
pp. 315-323 ◽  
Author(s):  
Glenn Wehtje ◽  
Larry J. Littlefield ◽  
David E. Zimmer
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Host Cell ◽  
Epidermal Cell ◽  
Cortical Cell ◽  
Hypersensitive Reaction ◽  
Host Cells ◽  
Plasmopara Halstedii ◽  
Host Cell Wall ◽  
Host Plasma Membrane

Penetration of sunflower, Heliantluis animus, root epidermal cells by zoospores of Plasmopara halstedii is preceded by formation of a papilla on the inner surface of the host cell wall that invaginates the host plasma membrane. Localized degradation and penetration of the host cell wall by the pathogen follow. The invading fungus forms an allantoid primary infection vesicle in the penetrated epidermal cell. The host plasma membrane invaginates around the infection vesicle but its continuity is difficult to follow. Upon exit from the epidermal cell the fungus may grow intercellularly, producing terminal haustorial branches which extend into adjacent host cells. The fungus may grow through one or two cortical cell is after growing from the epidermal cell before it becomes intercellular. Host plasma membrane is not penetrated by haustoria. Intercellular hyphae grow toward the apex of the plant and ramify the seedling tissue. Resistance in an immune cultivar is hypersensitive and is triggered upon contact of the host cell with the encysting zoospore before the host cell wall is penetrated. Degeneration of zoospore cytoplasm accompanies the hypersensitive reaction of the host. Zoospores were often parasitized by bacteria and did not germinate unless penicillin and streptomycin were added to the inoculum suspension.

scholarly journals Plasma membrane/cell wall perturbation activates a novel cell cycle checkpoint during G1 inSaccharomyces cerevisiae

2016 ◽  
Vol 113 (25) ◽  
pp. 6910-6915 ◽  
Author(s):  
Keiko Kono ◽  
Amr Al-Zain ◽  
Lea Schroeder ◽  
Makoto Nakanishi ◽  
Amy E. Ikui
Keyword(s):  
Cell Cycle ◽  
Wound Healing ◽  
Cell Wall ◽  
Plasma Membrane ◽  
Dna Replication ◽  
Membrane Damage ◽  
Cell Cycle Checkpoint ◽  
Plasma Membrane Damage ◽  
Cycle Checkpoint ◽  
Membrane Cell

Cellular wound healing or the repair of plasma membrane/cell wall damage (plasma membrane damage) occurs frequently in nature. Although various cellular perturbations, such as DNA damage, spindle misalignment, and impaired daughter cell formation, are monitored by cell cycle checkpoint mechanisms in budding yeast, whether plasma membrane damage is monitored by any of these checkpoints remains to be addressed. Here, we define the mechanism by which cells sense membrane damage and inhibit DNA replication. We found that the inhibition of DNA replication upon plasma membrane damage requires GSK3/Mck1-dependent degradation of Cdc6, a component of the prereplicative complex. Furthermore, the CDK inhibitor Sic1 is stabilized in response to plasma membrane damage, leading to cell integrity maintenance in parallel with the Mck1-Cdc6 pathway. Cells defective in both Cdc6 degradation and Sic1 stabilization failed to grow in the presence of plasma membrane damage. Taking these data together, we propose that plasma membrane damage triggers G1 arrest via Cdc6 degradation and Sic1 stabilization to promote the cellular wound healing process.

Subcellular location of phage infection protein (Pip) inLactococcus lactis

2006 ◽  
Vol 52 (7) ◽  
pp. 664-672 ◽  
Author(s):  
Duane T Mooney ◽  
Monica Jann ◽  
Bruce L Geller
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Lactococcus Lactis ◽  
Plasma Membranes ◽  
Gradient Centrifugation ◽  
Subcellular Location ◽  
Recognition Site ◽  
Phage Infection ◽  
Sucrose Density Gradient Centrifugation ◽  
Membrane Spanning

The amino acid sequence of the phage infection protein (Pip) of Lactococcus lactis predicts a multiple-membrane-spanning region, suggesting that Pip may be anchored to the plasma membrane. However, a near-consensus sortase recognition site and a cell wall anchoring motif may also be present near the carboxy terminus. If functional, this recognition site could lead to covalent linkage of Pip to the cell wall. Pip was detected in both plasma membranes and envelopes (plasma membrane plus peptidoglycan) isolated from the wild-type Pip strain LM2301. Pip was firmly attached to membrane and envelope preparations and was solubilized only by treatment with detergent. Three mutant Pip proteins were separately made in which the multiple-membrane-spanning region was deleted (Pip-Δmmsr), the sortase recognition site was converted to the consensus (Pip-H841G), or the sortase recognition site was deleted (Pip-Δ6). All three mutant Pip proteins co-purified with membranes and could not be solubilized except with detergent. When membranes containing Pip-Δmmsr were sonicated and re-isolated by sucrose density gradient centrifugation, Pip-Δmmsr remained associated with the membranes. Strains that expressed Pip-H841G or Pip-Δ6 formed plaques with near unit efficiency, whereas the strain that expressed Pip-Δmmsr did not form plaques of phage c2. Both membranes and cell-free culture supernatant from the strain expressing Pip-Δmmsr inactivated phage c2. These results suggest that Pip is an integral membrane protein that is not anchored to the cell wall and that the multiple-membrane-spanning region is required for productive phage infection but not phage inactivation.Key words: phage infection protein, Pip, Lactococcus lactis, subcellular location.

scholarly journals Identification and localization of cholecystokinin-binding sites on rat pancreatic plasma membranes and acinar cells: a biochemical and autoradiographic study.

1983 ◽  
Vol 96 (5) ◽  
pp. 1288-1297 ◽  
Author(s):  
S A Rosenzweig ◽  
L J Miller ◽  
J D Jamieson
Keyword(s):  
Acinar Cell ◽  
Binding Sites ◽  
Plasma Membranes ◽  
Acinar Cells ◽  
Pancreatic Acinar Cells ◽  
Cross Linking ◽  
Dependent Manner ◽  
Electron Microscopic ◽  
Electron Microscopic Autoradiography ◽  
Pancreatic Acini

Using the combined approaches of affinity labeling and light and electron microscopic autoradiography, we investigated the identification and localization of cholecystokinin (CCK)-binding sites on rat pancreatic acinar cells. To define the molecular properties of the CCK-binding site, we incubated rat pancreatic plasma membranes with 125-I-CCK-33 for 15 min at 23 degrees C followed by washing and cross-linking with disuccinimidyl suberate. Specific labeling of a major Mr 85,000 component was revealed as assessed by SDS PAGE under reducing conditions and autoradiography of the dried gels. Components of Mr greater than 200,000, Mr 130,000-140,000, and, Mr 55,000 were labeled under maximal cross-linking conditions. The labeling of all components was specifically inhibited by CCK-8 in a dose-dependent manner (Kd approximately 9 nM). The Mr 85,000 component had identical electrophoretic mobilities under reducing and nonreducing conditions indicating that it likely does not contain intramolecular disulfide bonds. The larger labeled species may be cross-linked oligomers of this binding protein or complexes between it and neighboring polypeptides. For studies on the distribution of CCK-binding sites, pancreatic acini were incubated with 125I-CCK-33 (0.1 nM) in the absence or presence of CCK-8 (1 microM) for 2 or 15 min at 37 degrees C, washed, and fixed in 2% glutaraldehyde. Quantitative autoradiographic analysis indicated that approximately 60% of the total grains were located within +/- 1 HD (1 HD = 100 nm) of the lateral and basal plasmalemma with little or no labeling of the apical plasmalemma. From these data, it was estimated that each acinar cell possesses at least 5,000-10,000 CCK-binding sites on its basolateral plasmalemma. The remaining grains showed no preferential concentration over the cytoplasm or nucleus. Together, these data indicate that CCK interacts with a Mr 85,000 protein located on the basolateral plasmalemma of the pancreatic acinar cell.

Ultrastructural changes of the plasmalemma and the cell wall during the life cycle of Cyanidium caldarium

1968 ◽  
Vol 171 (1023) ◽  
pp. 249-259 ◽  
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Life Cycle ◽  
Cell Division ◽  
Surface Pattern ◽  
Ultrastructural Changes ◽  
Adjacent Cell ◽  
Cyanidium Caldarium ◽  
Stage Of Development ◽  
Dominant Feature

During the life cycle of the unicellular alga Cyanidium caldarium the surfaces of the plasmalemma and the adjacent cell wall develop a number of differentiated structures which can be demonstrated with the freeze-etching technique. While cell division takes place, the plasma membrane is undifferentiated and covered with randomly distributed 55 and 80 Å particles as well as small holes from torn out particles that can be found adhering to the adjacent cell wall. The 80 Å particles possess a substructure and sometimes 40 Å fibrils can be seen leading from these particles into the cell wall. Just after cell division, shallow depressions showing a hexagonal surface pattern with a spacing of 105 Å and arrays of approximately hexagonally packed 55 Å particles are formed on the plasmalemma. The corresponding structures found on the cell wall are particle-studded humps, which fit into the shallow depressions, and faintly striated regions, which match the 55 Å particle arrays. During the next stage of development, the hexagonally patterned shallow depressions on the plasma membrane are transformed into regularly striated 300 to 350 Å wide and approximately 250 Å deep folds, while the arrays of 55 Å particles increase in size. On the adjacent cell wall we can follow the development of the particle-studded humps into ridges covered with 70 Å particles. The plasmalemma of old mature cells is characterized by long striated folds that replace nearly all network structured depressions, and a few small arrays of 55 Å particles. Long ridges covered with particles are the corresponding dominant feature on the inside of the cell wall. Prior to cell division, the striated folds and the other differentiations of the plasmalemma are broken down and eventually disappear so that the cell has again an undifferentiated ‘embryonic’ plasma membrane for cell division. Simultaneously the differentiated structures on the cell wall disappear. All the described particles and units forming plasma membrane differentiations seem to be confined to the surface layer of the plasmalemma. The outlined development cycle of the plasmalemma of Cyanidium shows that biological membranes have the potential to differentiate in time and space.

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