The ultrastructure of Methanothrix concilii, a mesophilic aceticlastic methanogen

1986 ◽  
Vol 32 (9) ◽  
pp. 703-710 ◽  
Author(s):  
Terry J. Beveridge ◽  
Girish B. Patel ◽  
Bob J. Harris ◽  
G. Dennis Sprott
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Circular Plates ◽  
A Cell ◽  
Granular Matrix ◽  
A Chain ◽  
The Individual

Methanothrix concilii strain GP6 consists of a chain of rod-shaped cells, ca. 2.5 μm in length and 0.8 μm in width, which are encased in a tubular proteinaceous sheath. The sheath is composed of annular hoops, ca. 8.0 nm wide and 9.0 nm thick, which are stacked together to form the tube. The ends of the sheath, and therefore the cell filament, are blocked by single, multilayered, 13.5 nm thick, circular plates, designated as "spacer plugs," which contain a series of concentric rings; these also separate the individual cells within each filament. Each cell is therefore bounded by a tubular section of sheath and two spacer plugs. Completely encapsulating each cell, and lying between the sheath and cell, is an amorphous granular matrix. Overlying the plasma membrane and surrounding each protoplast is a thin veil of material which resembles a cell wall, but which is unable to maintain the rod shape when cells are extruded from the sheath.

The Cell's Biological Rods and Ropes

MRS Bulletin ◽  
1999 ◽  
Vol 24 (10) ◽  
pp. 27-31 ◽  
Author(s):  
David Boal
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Chemical Composition ◽  
Intermediate Filaments ◽  
Plant Cells ◽  
Cell Type ◽  
Animal Cells ◽  
Limited Variation ◽  
A Cell ◽  
Mechanical Elements

Despite a variety of shapes and sizes, the generic mechanical structure of cells is remarkably similar from one cell type to the next. All cells are bounded by a plasma membrane, a fluid sheet that controls the passage of materials into and out of the cell. Plant cells and bacteria reinforce this membrane with a cell wall, permitting the cell to operate at an elevated osmotic pressure. Simple cells, such as the bacterium shown in Figure 1a, possess a fairly homogeneous interior containing the cell's genetic blueprint and protein workhorses, but no mechanical elements. In contrast, as can be seen in Figure 1b, plant and animal cells contain internal compartments and a filamentous cytoskeleton—a network of biological ropes, cables, and poles that helps maintain the cell's shape and organize its contents.Four principal types of filaments are found in the cytoskeleton: spectrin, actin, microtubules, and a family of intermediate filaments. Not all filaments are present in all cells. The chemical composition of the filaments shows only limited variation from one cell to another, even in organisms as diverse as humans and yeasts. Membranes have a more variable composition, consisting of a bi-layer of dual-chain lipid molecules in which are embedded various proteins and frequently a moderate concentration of cholesterol. The similarity of the cell's mechanical elements in chemical composition and physical characteristics encourages us to search for universal strategies that have developed in nature for the engineering specifications of the cell. In this article, we concentrate on the cytoskeleton and its filaments.

scholarly journals A pathway for cell wall anchorage of Saccharomyces cerevisiae alpha-agglutinin.

1994 ◽  
Vol 14 (7) ◽  
pp. 4825-4833 ◽  
Author(s):  
C F Lu ◽  
J Kurjan ◽  
P N Lipke
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Plasma Membrane ◽  
Cell Surface ◽  
Soluble Form ◽  
Gpi Anchor ◽  
Glycosyl Phosphatidylinositol ◽  
Experimental Support ◽  
Cell Biol ◽  
A Cell

Saccharomyces cerevisiae alpha-agglutinin is a cell wall-anchored adhesion glycoprotein. The previously identified 140-kDa form, which contains a glycosyl-phosphatidylinositol (GPI) anchor (D. Wojciechowicz, C.-F. Lu, J. Kurjan, and P. N. Lipke, Mol. Cell. Biol. 13:2554-2563, 1993), and additional forms of 80, 150, 250 to 300, and > 300 kDa had the properties of intermediates in a transport and cell wall anchorage pathway. N glycosylation and additional modifications resulted in successive increases in size during transport. The 150- and 250- to 300-kDa forms were membrane associated and are likely to be intermediates between the 140-kDa form and a cell surface GPI-anchored form of > 300 kDa. A soluble form of > 300 kDa that lacked the GPI anchor had properties of a periplasmic intermediate between the plasma membrane form and the > 300-kDa cell wall-anchored form. These results constitute experimental support for the hypothesis that GPI anchors act to localize alpha-agglutinin to the plasma membrane and that cell wall anchorage involves release from the GPI anchor to produce a periplasmic intermediate followed by linkage to the cell wall.

Recruitment of myosin VIII towards plastid surfaces is root-cap specific and provides the evidence for actomyosin involvement in root osmosensing

2005 ◽  
Vol 32 (8) ◽  
pp. 721 ◽  
Author(s):  
Przemysław Wojtaszek ◽  
Anna Anielska-Mazur ◽  
Halina Gabryś ◽  
František Baluška ◽  
Dieter Volkmann
Keyword(s):  
Cell Wall ◽  
Root Cap ◽  
Volume Control ◽  
Animal Cells ◽  
Active Involvement ◽  
A Cell ◽  
Osmotic Stimulus ◽  
Tight Association ◽  
The Individual ◽  
Cellular Compartments

The existence of a cell wall–plasma membrane–cytoskeleton (WMC) continuum in plants has long been postulated. However, the individual molecules building such a continuum are still largely unknown. We test here the hypothesis that the integrin-based multiprotein complexes of animal cells have been replaced in plants with more dynamic entities. Using an experimental approach based on protoplast digestion mixtures, and utilising specific antibodies against Arabidopsis ATM1 myosin, we reveal possible roles played by plant-specific unconventional myosin VIII in the functioning of WMC continuum. We demonstrate rapid relocation (less than 5 min) of myosin VIII to statolith surfaces in maize root-cap cells, which is accompanied by the reorganisation of actin cytoskeleton. Upon prolonged stimulation, myosin VIII is also recruited to plasmodesmata and pit-fields of plasmolysing root cap statocytes. The osmotic stimulus is the major factor inducing relocation, but the cell wall–cytoskeleton interactions also play an important role. In addition, we demonstrate the tight association of myosin VIII with the surfaces of chloroplasts, and provide an indication for the differences in the mechanisms of plastid movement in roots and leaves of plants. Overall, our data provide evidence for the active involvement of actomyosin complexes, rooted in the WMC continuum, in the cellular volume control and maintenance of spatial relationships between cellular compartments.

scholarly journals Lack of GTP-bound Rho1p in secretory vesicles of Saccharomyces cerevisiae

2003 ◽  
Vol 162 (1) ◽  
pp. 85-97 ◽  
Author(s):  
Mitsuhiro Abe ◽  
Hiroshi Qadota ◽  
Aiko Hirata ◽  
Yoshikazu Ohya
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Plasma Membrane ◽  
Vesicular Transport ◽  
Secretory Vesicles ◽  
Glucan Synthase ◽  
Exchange Factor ◽  
Inactive Form ◽  
A Cell

Rho1p, an essential Rho-type GTPase in Saccharomyces cerevisiae, activates its effectors in the GTP-bound form. Here, we show that Rho1p in secretory vesicles cannot activate 1,3-β-glucan synthase, a cell wall synthesizing enzyme, during vesicular transport to the plasma membrane. Analyses with an antibody preferentially reacting with the GTP-bound form of Rho1p revealed that Rho1p remains in the inactive form in secretory vesicles. Rom2p, the GDP/GTP exchange factor of Rho1p, is preferentially localized on the plasma membrane even when vesicular transport is blocked. Overexpression of Rom2p results in delocalization of Rom2p and accumulation of 1,3-β-glucan in secretory vesicles. Based on these results, we propose that Rho1p is kept inactive in intracellular secretory organelles, resulting in repression of the activity of the cell wall–synthesizing enzyme within cells.

A pathway for cell wall anchorage of Saccharomyces cerevisiae alpha-agglutinin

1994 ◽  
Vol 14 (7) ◽  
pp. 4825-4833
Author(s):  
C F Lu ◽  
J Kurjan ◽  
P N Lipke
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Plasma Membrane ◽  
Cell Surface ◽  
Soluble Form ◽  
Gpi Anchor ◽  
Glycosyl Phosphatidylinositol ◽  
Experimental Support ◽  
Cell Biol ◽  
A Cell

Saccharomyces cerevisiae alpha-agglutinin is a cell wall-anchored adhesion glycoprotein. The previously identified 140-kDa form, which contains a glycosyl-phosphatidylinositol (GPI) anchor (D. Wojciechowicz, C.-F. Lu, J. Kurjan, and P. N. Lipke, Mol. Cell. Biol. 13:2554-2563, 1993), and additional forms of 80, 150, 250 to 300, and > 300 kDa had the properties of intermediates in a transport and cell wall anchorage pathway. N glycosylation and additional modifications resulted in successive increases in size during transport. The 150- and 250- to 300-kDa forms were membrane associated and are likely to be intermediates between the 140-kDa form and a cell surface GPI-anchored form of > 300 kDa. A soluble form of > 300 kDa that lacked the GPI anchor had properties of a periplasmic intermediate between the plasma membrane form and the > 300-kDa cell wall-anchored form. These results constitute experimental support for the hypothesis that GPI anchors act to localize alpha-agglutinin to the plasma membrane and that cell wall anchorage involves release from the GPI anchor to produce a periplasmic intermediate followed by linkage to the cell wall.

scholarly journals Prm1 Prevents Contact-Dependent Lysis of Yeast Mating Pairs

2004 ◽  
Vol 3 (6) ◽  
pp. 1664-1673 ◽  
Author(s):  
Hui Jin ◽  
Candice Carlile ◽  
Scott Nolan ◽  
Eric Grote
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Membrane Fusion ◽  
Yeast Cells ◽  
Osmotic Gradient ◽  
Fusion Event ◽  
Mating Partner ◽  
Yeast Mating ◽  
Cell Wall Remodeling ◽  
A Cell

ABSTRACT Membrane fusion requires localized destabilization of two phospholipid bilayers, but unrestrained membrane destabilization could result in lysis. prm1 mutant yeast cells have a defect at the plasma membrane fusion stage of mating that typically results in the accumulation of prezygotes that have fingers of membrane-bound cytoplasm projecting from one cell of each pair into its mating partner in the direction of the osmotic gradient between the cells. However, some prm1 mating pairs fuse successfully whereas the two cells in other prm1 mating pairs simultaneously lyse. Lysis only occurs if both mating partners are prm1 mutants. Osmotic stabilization does not protect prm1 mating pairs from lysis, indicating that lysis is not caused by a cell wall defect. prm1 mating pairs without functional mitochondria still lyse, ruling out programmed cell death. No excess lysis was found after pheromone treatment of haploid prm1 cells, and lysis did not occur in mating pairs when prm1 was combined with the fus1 and fus2 mutations to block cell wall remodeling. Furthermore, short (<1 μm) cytoplasmic microfingers indicating the completion of cell wall remodeling appeared immediately before lysis. In combination, these results demonstrate that plasma membrane contact is a prerequisite for lysis. Cytoplasmic microfingers are unlikely to cause lysis since most prm1 mating pairs with microfingers do not lyse, and microfingers were also detected before fusion in some wild-type mating pairs. The lysis of prm1 mutant mating pairs suggests that the Prm1 protein stabilizes the membrane fusion event of yeast mating.

scholarly journals Parallel secretory pathways to the cell surface in yeast.

1995 ◽  
Vol 131 (2) ◽  
pp. 297-310 ◽  
Author(s):  
E Harsay ◽  
A Bretscher
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Double Mutant ◽  
Average Diameter ◽  
Plasma Membrane Atpase ◽  
Membrane Atpase ◽  
A Cell ◽  
Exocytic Pathway ◽  
Two Populations ◽  
Wall Components

Saccharomyces cerevisiae mutants that have a post-Golgi block in the exocytic pathway accumulate 100-nm vesicles carrying secretory enzymes as well as plasma membrane and cell-wall components. We have separated the vesicle markers into two groups by equilibrium isodensity centrifugation. The major population of vesicles contains Bg12p, an endoglucanase destined to be a cell-wall component, as well as Pma1p, the major plasma membrane ATPase. In addition, Snc1p, a synaptobrevin homologue, copurifies with these vesicles. Another vesicle population contains the periplasmic enzymes invertase and acid phosphatase. Both vesicle populations also contain exoglucanase activity; the major exoglucanase normally secreted from the cell, encoded by EXG1, is carried in the population containing periplasmic enzymes. Electron microscopy shows that both vesicle groups have an average diameter of 100 nm. The late secretory mutants sec1, sec4, and sec6 accumulate both vesicle populations, while neither is detected in wild-type cells, early sec mutants, or a sec13 sec6 double mutant. Moreover, a block in endocytosis does not prevent the accumulation of either vesicle species in an end4 sec6 double mutant, further indicating that both populations are of exocytic origin. The accumulation of two populations of late secretory vesicles indicates the existence of two parallel routes from the Golgi to the plasma membrane.

scholarly journals Ultrastructure and Peripheral Membranes of the Mycetomal Microorganisms of Sitophilus granarius (L.) (Coleoptera)

1966 ◽  
Vol 1 (2) ◽  
pp. 181-186
Author(s):  
I. GRINYER ◽  
A. J. MUSGRAVE
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Electron Microscope ◽  
Sitophilus Granarius ◽  
Large Numbers ◽  
A Cell ◽  
Intracellular Organelles ◽  
Micro Organisms

The peripheral membranes of the micro-organisms of the mycetocytes of adult midgut caecae and of larval mycetomes of Sitophilus granarius (L.), GG strain, have been examined with an electron microscope. The majority of the mycetocytes were depleted of intracellular organelles but contained large numbers of mycetomal micro-organisms, most of which exhibited only one peripheral membrane. Some mycetocytes, however, had well-developed ultrastructure and harboured mycetomal micro-organisms which showed two peripheral membranes, namely a cell wall and plasma membrane. Intermediate conditions also occurred. It is suggested that the absence of host-provided membranes around the micro-organisms categorizes them as obligate symbiotes.

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