THE ORGANIZATION OF CYTOPLASMIC COMPONENTS DURING THE PHASE OF CELL WALL THICKENING IN DIFFERENTIATING CAMBIAL DERIVATIVES OF ACER RUBRUM

1965 ◽  
Vol 43 (11) ◽  
pp. 1401-1407 ◽  
Author(s):  
James Cronshaw
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Wall ◽  
Plasma Membrane ◽  
Osmium Tetroxide ◽  
Acer Rubrum ◽  
Middle Layer ◽  
Wall Thickening ◽  
Cytoplasmic Microtubules ◽  
Derivatives Of ◽  
Peripheral Cytoplasm

Cambial derivatives of Acer rubrum have been examined at stages of their differentiation following fixation in 3% or 6% glutaraldehyde with a post fixation in osmium tetroxide. At early stages of development numerous free ribosomes are present in the cytoplasm, and elements of the endoplasmic reticulum tend to align themselves parallel to the cell surfaces. The plasma membrane is closely applied to the cell walls. During differentiation a complex system of cytoplasmic microtubules develops in the peripheral cytoplasm. These microtubules are oriented, mirroring the orientation of the most recently deposited microfibrils of the cell wall. The microtubules form a steep helix in the peripheral cytoplasm at the time of deposition of the middle layer of the secondary wall. During differentiation the free ribosomes disappear from the cytoplasm and numerous elements of rough endoplasmic reticulum with associated polyribosomes become more evident. In many cases the endoplasmic reticulum is associated with the cell surface. During the later stages of differentiation there are numerous inclusions between the cell wall and the plasma membrane.

scholarly journals Subcellular localization of cellulases in auxin-treated pea.

1976 ◽  
Vol 69 (1) ◽  
pp. 97-105 ◽  
Author(s):  
A K Bal ◽  
D P Verma ◽  
H Byrne ◽  
G A Maclachlan
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Wall ◽  
Plasma Membrane ◽  
Major Part ◽  
Osmium Tetroxide ◽  
Close Association ◽  
Cellulase Activity ◽  
Cytochemical Localization ◽  
Tissue Sections ◽  
Inner Surface

Two forms of cellulase, buffer soluble (BS) and buffer insoluble (BI), are induced as a result of auxin treatment of dark-grown pea epicotyls. These two cellulases have been purified to homogeneity. Antibodies raised against the purified cellulases were conjugated with ferritin and were used to localize the two cellulases. Tissue sections were fixed in cold paraformaldehyde-glutaraldehyde and incubated for 1 h in the ferritin conjugates. The sections were washed with continuous shaking for 18 h and subsequently postfixed in osmium tetroxide. Tissue incubated in unconjugated ferritin was used as a control. A major part of BI cellulase is localized at the inner surface of the cell wall in close association with microfibrils. BS cellulase is localized mainly within the distended endoplasmic reticulum. Gogli complex and plasma membrane appear to be completely devoid of any cellulase activity. These observations are consistent with cytochemical localization and biochemical data on the distribution of these two cellulases among various cell and membrane fractions.

scholarly journals THE FINE STRUCTURE OF DIFFERENTIATING XYLEM ELEMENTS

1965 ◽  
Vol 24 (3) ◽  
pp. 415-431 ◽  
Author(s):  
James Cronshaw ◽  
G. Benjamin Bouck
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Wall ◽  
Fine Structure ◽  
Secondary Wall ◽  
Osmium Tetroxide ◽  
Light And Electron Microscopy ◽  
Wall Thickening ◽  
Direction Parallel ◽  
Secondary Wall Thickening ◽  
Xylem Elements

Differentiating xylem elements of Avena coleoptiles have been examined by light and electron microscopy. Fixation in 2 per cent phosphate-buffered osmium tetroxide and in 6 per cent glutaraldehyde, followed by 2 per cent osmium tetroxide, revealed details of the cell wall and cytoplasmic fine structure. The localized secondary wall thickening identified the xylem elements and indicated their state of differentiation. These differentiating xylem elements have dense cytoplasmic contents in which the dictyosomes and elements of rough endoplasmic reticulum are especially numerous. Vesicles are associated with the dictyosomes and are found throughout the cytoplasm. In many cases, these vesicles have electron-opaque contents. "Microtubules" are abundant in the peripheral cytoplasm and are always associated with the secondary wall thickenings. These microtubules are oriented in a direction parallel to the microfibrillar direction of the thickenings. Other tubules are frequently found between the cell wall and the plasma membrane. Our results support the view that the morphological association of the "microtubules" with developing cell wall thickenings may have a functional significance, especially with respect to the orientation of the microfibrils. Dictyosomes and endoplasmic reticulum may have a function in some way connected with the synthetic mechanism of cell wall deposition.

scholarly journals Four distinct secretory pathways serve protein secretion, cell surface growth, and peroxisome biogenesis in the yeast Yarrowia lipolytica.

1997 ◽  
Vol 17 (9) ◽  
pp. 5210-5226 ◽  
Author(s):  
V I Titorenko ◽  
D M Ogrydziak ◽  
R A Rachubinski
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Wall ◽  
Plasma Membrane ◽  
Protein Secretion ◽  
Peroxisome Biogenesis ◽  
Peroxisomal Membrane ◽  
Mycelial Form ◽  
Secretory Pathways ◽  
Associated Proteins ◽  
Yeast Yarrowia Lipolytica

We have identified and characterized mutants of the yeast Yarrowia lipolytica that are deficient in protein secretion, in the ability to undergo dimorphic transition from the yeast to the mycelial form, and in peroxisome biogenesis. Mutations in the SEC238, SRP54, PEX1, PEX2, PEX6, and PEX9 genes affect protein secretion, prevent the exit of the precursor form of alkaline extracellular protease from the endoplasmic reticulum, and compromise peroxisome biogenesis. The mutants sec238A, srp54KO, pex2KO, pex6KO, and pex9KO are also deficient in the dimorphic transition from the yeast to the mycelial form and are affected in the export of only plasma membrane and cell wall-associated proteins specific for the mycelial form. Mutations in the SEC238, SRP54, PEX1, and PEX6 genes prevent or significantly delay the exit of two peroxisomal membrane proteins, Pex2p and Pex16p, from the endoplasmic reticulum en route to the peroxisomal membrane. Mutations in the PEX5, PEX16, and PEX17 genes, which have previously been shown to be essential for peroxisome biogenesis, affect the export of plasma membrane and cell wall-associated proteins specific for the mycelial form but do not impair exit from the endoplasmic reticulum of either Pex2p and Pex16p or of proteins destined for secretion. Biochemical analyses of these mutants provide evidence for the existence of four distinct secretory pathways that serve to deliver proteins for secretion, plasma membrane and cell wall synthesis during yeast and mycelial modes of growth, and peroxisome biogenesis. At least two of these secretory pathways, which are involved in the export of proteins to the external medium and in the delivery of proteins for assembly of the peroxisomal membrane, diverge at the level of the endoplasmic reticulum.

Lomasome biogenesis and function in armillaria mellea

1978 ◽  
Vol 36 (2) ◽  
pp. 402-403
Author(s):  
B. Ch. Behboodi
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Osmium Tetroxide ◽  
Higher Plants ◽  
Cell Wall Formation ◽  
Extensive Investigation ◽  
Sodium Cacodylate ◽  
Armillaria Mellea ◽  
Synthetic Media ◽  
And Function

IntroductionBorder bodies or lomasomes are the aggregation of membranes and vesicles located between the plasma membrane and the cell wall of many fungi, algae, and higher plants. Despite extensive investigation, the biogenesis as well as function of these structures is not yet known. The purpose of this investigation was to describe the biogenesis of lomasomes in Armillaria mellea and to provide some observations on their function related to cell wall formation.Materials and MethodsVarious thalli of fungi as non-aggregated hyphae, pseudosclerotes, rhizomorphs and carpophores were grown either on orange or synthetic media as described previously. The thalli were fixed in 4% glutaraldehyde buffered with 0.1 M sodium cacodylate (pH 7.4), and 0.15 M sucrose for 4 h at 4°. They were postfixed with 1% osmium tetroxide in the same buffer for 2 h at 4° and embedded in Epon according to the Luft procedure. Cytochemical studies using thiocarbohydrazide-silver proteinate were performed according the Thiéry.

scholarly journals Intercellular trafficking via plasmodesmata: molecular layers of complexity

2020 ◽  
Author(s):  
Ziqiang Patrick Li ◽  
Andrea Paterlini ◽  
Marie Glavier ◽  
Emmanuelle M. Bayer
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Wall ◽  
Plasma Membrane ◽  
Plant Cells ◽  
Functional Domains ◽  
Dynamic Interactions ◽  
Intercellular Trafficking ◽  
Multiple Routes ◽  
Molecular Components ◽  
Molecular Layers

Abstract Plasmodesmata are intercellular pores connecting together most plant cells. These structures consist of a central constricted form of the endoplasmic reticulum, encircled by some cytoplasmic space, in turn delimited by the plasma membrane, itself ultimately surrounded by the cell wall. The presence and structure of plasmodesmata create multiple routes for intercellular trafficking of a large spectrum of molecules (encompassing RNAs, proteins, hormones and metabolites) and also enable local signalling events. Movement across plasmodesmata is finely controlled in order to balance processes requiring communication with those necessitating symplastic isolation. Here, we describe the identities and roles of the molecular components (specific sets of lipids, proteins and wall polysaccharides) that shape and define plasmodesmata structural and functional domains. We highlight the extensive and dynamic interactions that exist between the plasma/endoplasmic reticulum membranes, cytoplasm and cell wall domains, binding them together to effectively define plasmodesmata shapes and purposes.

scholarly journals ON THE FINE STRUCTURE OF THE CAMBIUM OF FRAXINUS AMERICANA L

1966 ◽  
Vol 31 (1) ◽  
pp. 79-93 ◽  
Author(s):  
Lalit M. Srivastava
Keyword(s):  
Endoplasmic Reticulum ◽  
Fine Structure ◽  
Osmium Tetroxide ◽  
Coated Vesicles ◽  
Fraxinus Americana ◽  
Parenchyma Cells ◽  
Rough Er ◽  
Cambial Cells ◽  
Peripheral Cytoplasm

The fine structure of ash cambium was studied after glutaraldehyde-osmium tetroxide fixation. The fusiform and ray initials are essentially alike, and both have the basic complement of organelles and membranes typical of parenchyma cells. The varied behavior of the two types of initials and the role of cambium in oriented production of the xylem and phloem are still unexplained phenomena. Actively growing cambial cells are highly vacuolate. They are rich in endoplasmic reticulum of the rough cisternal form, ribosomes, dictyosomes, and coated vesicles. Microtubules are present in the peripheral cytoplasm. The plasmalemma appears to be continuous with the endoplasmic reticulum and produces coated vesicles as well as micropinocytotic vesicles with smooth surfaces. The plastids have varying amounts of an intralamellar inclusion which may be a lipoprotein. The quiescent cambium is deficient in rough ER and coated vesicles and has certain structures which may be condensed proteins.

Certain aspects of xylem differentiation in corn

1972 ◽  
Vol 50 (9) ◽  
pp. 1795-1804 ◽  
Author(s):  
L. M. Srivastava ◽  
A. P. Singh
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Wall ◽  
Wall Thickening ◽  
Xylem Differentiation ◽  
Cytoplasmic Protein ◽  
Wall Deposition ◽  
Vessel Elements ◽  
Parenchyma Cells ◽  
Vacuolar Membranes

Differentiation of vessel elements in corn is accompanied by marked changes in nearly all organelles except plastids. The young cells increase in volume and apparently synthesize new cytoplasmic protein. The initiation of wall thickening is accompanied by an aggregation of microtubules in specific locations and an increase in the number of mitochondria and dictyosomes. During the period of active wall deposition, the endoplasmic reticulum (ER) shows a highly elaborate form, harbors intralamellar tubules, and nearly blankets those parts of the wall which remain unthickened. Dictyosomes seem to produce at least two types of vesicles, one of which may serve as a carrier of lignin precursors. The final autolysis involves a progressive removal of vacuolar membranes, plastids, dictyosomes, vesicles associated with secretion of noncellulosic polysaccharides, microtubules, and finally plasmalemma, parts of cell wall, and cytoplasm. Mitochondria and ribosomes are degenerated. The ER probably plays an important role in this autolysis. The parenchyma cells associated with vessel elements are rich in mitochondria.

scholarly journals Abnormal sterol-induced cell wall glucan deficiency in yeast is due to impaired glucan synthase transport to the plasma membrane

2020 ◽  
Vol 477 (24) ◽  
pp. 4729-4744
Author(s):  
L. Roxana Gutierrez-Armijos ◽  
Rodrigo A. C. Sussmann ◽  
Ariel M. Silber ◽  
Mauro Cortez ◽  
Agustín Hernández
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Wall ◽  
Plasma Membrane ◽  
Cell Walls ◽  
Bone Development ◽  
Cholesterol Biosynthesis ◽  
Cellular Functions ◽  
Fungal Cell ◽  
Glucan Synthase ◽  
Unconventional Secretion

Abnormal sterols disrupt cellular functions through yet unclear mechanisms. In Saccharomyces cerevisiae, accumulation of Δ8-sterols, the same type of sterols observed in patients of Conradi–Hünermann–Happle syndrome or in fungi after amine fungicide treatment, leads to cell wall weakness. We have studied the influence of Δ8-sterols on the activity of glucan synthase I, the protein synthetizing the main polymer in fungal cell walls, its regulation by the Cell Wall Integrity (CWI) pathway, and its transport from the endoplasmic reticulum to the plasma membrane. We ascertained that the catalytic characteristics were mostly unaffected by the presence of abnormal sterols but the enzyme was partially retained in the endoplasmic reticulum, leading to glucan deficit at the cell wall. Furthermore, we observed that glucan synthase I traveled through an unconventional exocytic route to the plasma membrane that is associated with low density intracellular membranes. Also, we found out that the CWI pathway remained inactive despite low glucan levels at the cell wall. Taken together, these data suggest that Δ8-sterols affect cell walls by inhibiting unconventional secretion of proteins leading to retention and degradation of glucan synthase I, while the compensatory CWI pathway is unable to activate. These results could be instrumental to understand defects of bone development in cholesterol biosynthesis disorders and fungicide mechanisms of action.

scholarly journals Electron Microscopy of the Ovary of Fasciola Hepatica

1964 ◽  
Vol s3-105 (70) ◽  
pp. 213-218
Author(s):  
R. A. R. GRESSON
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Nuclear Envelope ◽  
Fasciola Hepatica ◽  
Amorphous Material ◽  
Primary Oocyte ◽  
Intercellular Region ◽  
Narrow Bridge ◽  
Peripheral Cytoplasm

The external wall of the ovary of Fasciola hepatica is a membrane-like structure in contact with a non-cellular material in the ovary. An intercellular region containing an amorphous material of moderate electron density is present in the ovary. The primary oocytes are provided with peripheral processes that extend into the intercellular region. The oocytes do not proceed beyond the prophase of the first meiotic division until after they leave the ovary. The nucleolus of the primary oocyte contains vacuole-like areas and emits granular material to the nucleoplasm; some of this material may move to the cytoplasm. Pores are present in the nuclear envelope. In older oocytes narrow bridge-like structures connect the nucleolus and the nuclear envelope. The nuclear envelope of the primary oocyte undergoes replication. It is continuous with the endoplasmic reticulum and the plasma membrane. The location of the mitochondria is correlated with the phases of growth of oogonia and oocytes. The mitochondria possess irregularly arranged cristae. Small, round or oval nutritive bodies are present in the peripheral cytoplasm of older oocytes. It is suggested that areas of relatively high density containing vacuole-like structures represent the Golgi complex.

scholarly journals Cellulose synthase complexes display distinct dynamic behaviors during xylem transdifferentiation

2018 ◽  
Vol 115 (27) ◽  
pp. E6366-E6374 ◽  
Author(s):  
Yoichiro Watanabe ◽  
Rene Schneider ◽  
Sarah Barkwill ◽  
Eliana Gonzales-Vigil ◽  
Joseph L. Hill ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Cell Expansion ◽  
Secondary Wall ◽  
Transition Period ◽  
Cellulose Synthase ◽  
Wall Thickening ◽  
Cellulose Synthesis ◽  
Primary Wall ◽  
Dynamic Behaviors

In plants, plasma membrane-embedded CELLULOSE SYNTHASE (CESA) enzyme complexes deposit cellulose polymers into the developing cell wall. Cellulose synthesis requires two different sets of CESA complexes that are active during cell expansion and secondary cell wall thickening, respectively. Hence, developing xylem cells, which first undergo cell expansion and subsequently deposit thick secondary walls, need to completely reorganize their CESA complexes from primary wall- to secondary wall-specific CESAs. Using live-cell imaging, we analyzed the principles underlying this remodeling. At the onset of secondary wall synthesis, the primary wall CESAs ceased to be delivered to the plasma membrane and were gradually removed from both the plasma membrane and the Golgi. For a brief transition period, both primary wall- and secondary wall-specific CESAs coexisted in banded domains of the plasma membrane where secondary wall synthesis is concentrated. During this transition, primary and secondary wall CESAs displayed discrete dynamic behaviors and sensitivities to the inhibitor isoxaben. As secondary wall-specific CESAs were delivered and inserted into the plasma membrane, the primary wall CESAs became concentrated in prevacuolar compartments and lytic vacuoles. This adjustment in localization between the two CESAs was accompanied by concurrent decreased primary wall CESA and increased secondary wall CESA protein abundance. Our data reveal distinct and dynamic subcellular trafficking patterns that underpin the remodeling of the cellulose biosynthetic machinery, resulting in the removal and degradation of the primary wall CESA complex with concurrent production and recycling of the secondary wall CESAs.

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