The route of entry of cytoplasmically synthesized proteins into chloroplasts of algae possessing chloroplast ER

1979 ◽  
Vol 35 (1) ◽  
pp. 253-266
Author(s):  
S.P. Gibbs
Keyword(s):  
Protein Synthesis ◽  
Nuclear Envelope ◽  
Outer Membrane ◽  
Chloroplast Envelope ◽  
Inhibit Protein Synthesis ◽  
Ochromonas Danica ◽  
Plastid Proteins ◽  
Regular Network ◽  
Cytoplasmic Ribosomes ◽  
Plastid Ribosomes

In 8 classes of algae, namely the Cryptophyceae, Raphidophyceae, Haptophyceae, Chrysophyceae, Bacillariophyceae, Xanthophyceae, Eustigmatophyceae and Phaeophyceae, the chloroplasts, in addition to being surrounded by a double-membraned chloroplast envelope, are also enclosed by a cisterna of endoplasmic reticulum called the chloroplast ER. Often this ER cisterna is continuous with the outher membrane of the nuclear envelope in such a manner that the nuclear envelope forms a part of the ER sac enclosing the chloroplast. In all these classes of algae except the Cryptophyceae, a regular network of tubules and vesicles, named the periplastidal reticulum, is present at a specific location between the chloroplast envelope and the chloroplast ER. In the Cryptophyceae, scattered vesicles are found between the chloroplast envelope and the chloroplast ER. Ribosomes which have been shown to be arranged to polysomes are found on the outer membrane of the chloroplast ER. It is proposed that nuclear-coded proteins which are destined for the chloroplast are synthesized on these polysomes, passing during synthesis into the lumen of the ER cisterna. Vesicles containing these proteins then pinch off the chloroplast ER and form the periplastidal reticulum. Vesicles containing these proteins then pinch off the chloroplast ER and form the periplastidal reticulum. Vesicles then fuse with the outer membrane of the chloroplast envelope thereby delivering their contents to the lumen of the chloroplast envelope. Proteins then cross the inner membrane of the chloroplast envelope in an as yet unknown manner. Experimental evidence for this hypothesis comes from studies on Ochromonas danica using chloramphenicol and spectinomycin, which inhibit protein synthesis on plastid ribosomes, and cycloheximide, which inhibits protein synthesis on cytoplasmic ribosomes. In cells of Ochromonas exposed to chloramphenicol or spectinomycin, the periplastidal reticulum proliferates markedly becoming several layers thick. Presumably this build up of periplastidal reticulum occurs because the transport of cytoplasmically synthesized plastid proteins is slowed down when protein synthesis in the chloroplast is inhibited. Conversely, when cells of Ochromonas are treated with cycloheximide, there is a reduction in the amount of periplastidal reticulum presumably because there are no cytoplasmically synthesized proteins to be transported into the chloroplast.

scholarly journals NUCLEAR ENVELOPE-CHLOROPLAST RELATIONSHIPS IN ALGAE

1962 ◽  
Vol 14 (3) ◽  
pp. 433-444 ◽  
Author(s):  
Sarah P. Gibbs
Keyword(s):  
Nuclear Envelope ◽  
Outer Membrane ◽  
Related Species ◽  
The Other ◽  
Chloroplast Envelope ◽  
Outer Envelope ◽  
Starch Grains ◽  
Ochromonas Danica ◽  
Narrow Space

In Ochromonas danica and two related species (Chrysophyceae) and in Rhodomonas lens and Cryptomonas sp. (Cryptophyceae), the chloroplast is surrounded by an outer double-membraned envelope which lies outside the usual double-membraned chloroplast envelope. At the borders of the area where the chloroplast lies adjacent to the nucleus, this outer envelope is continuous with the outer membrane of the nuclear envelope as a double-membraned outfolding, so that the entire chloroplast in these species lies within a double-membraned sac, one wall of which is the nuclear envelope. In Olisthodiscus sp. (Chrysophyceae ?), each of the small peripheral chloroplasts is surrounded by a similar double-membraned outer envelope, but in this species no connections with the nuclear envelope were observed. In the Ochromonadaceae, a characteristic array of tubules is present within the sac in the narrow space which separates the chloroplast from the nucleus. In the other species studied, tubules are present at places between the chloroplast envelope and the outer envelope. In the Cryptophyceae, the starch grains lie outside the chloroplast envelope, but within the outer double-membraned sac. A double-membraned outer envelope appears to be present outside the chloroplasts of the Phaeophyta and Euglenophyta, but seems to be absent in the other groups of algae.

scholarly journals EFFECTS OF CHLORAMPHENICOL ON CHLOROPLAST AND MITOCHONDRIAL ULTRASTRUCTURE IN OCHROMONAS DANICA

1972 ◽  
Vol 52 (3) ◽  
pp. 598-614 ◽  
Author(s):  
Heidi Smith-Johannsen ◽  
Sarah P. Gibbs
Keyword(s):  
Growth Rate ◽  
Ribosomal Proteins ◽  
Chloroplast Development ◽  
Chlorophyll Synthesis ◽  
Chloroplast Envelope ◽  
Mitochondrial Ultrastructure ◽  
Mitochondrial Ribosomes ◽  
Ochromonas Danica ◽  
Progressive Loss ◽  
Cytoplasmic Ribosomes

The effect of chloramphenicol (CAP) on cell division and organelle ultrastructure was studied during light-induced chloroplast development in the Chrysophyte alga, Ochromonas danica. Since the growth rate of the CAP-treated cells is the same as that of the control cells for the first 12 hr in the light, CAP is presumed to be acting during that interval solely by inhibiting protein synthesis on chloroplast and mitochondrial ribosomes. CAP markedly inhibits chloroplast growth and differentiation. During the first 12 hr in the light, chlorophyll synthesis is inhibited by 93%, the formation of new thylakoid membranes is reduced by 91%, and the synthesis of chloroplast ribosomes is inhibited by 81%. Other chloroplast-associated abnormalities which occur during the first 12 hr and become more pronounced with extended CAP treatment are the presence of prolamellar bodies and of abnormal stacks of thylakoids, the proliferation of the perinuclear reticulum, and the accumulation of dense granular material between the chloroplast envelope and the chloroplast endoplasmic reticulum. CAP also causes a progressive loss of the mitochondrial cristae, which is paralleled by a decline in the growth rate of the cells, but it has no effect on the synthesis of mitochondrial ribosomes. We postulate that one or more chloroplast ribosomal proteins are synthesized on chloroplast ribosomes, whereas mitochondrial ribosomal proteins are synthesized on cytoplasmic ribosomes.

INHIBITION OF THYROGLOBULIN BIOSYNTHESIS AND DEGRADATION BY EXCESS IODIDE. SYNERGISM WITH LITHIUM

1976 ◽  
Vol 81 (2) ◽  
pp. 495-506 ◽  
Author(s):  
A. Radvila ◽  
R. Roost ◽  
H. Bürgi ◽  
H. Kohler ◽  
H. Studer
Keyword(s):  
Protein Synthesis ◽  
Thyroid Gland ◽  
Inhibitory Action ◽  
Inhibit Protein Synthesis ◽  
Thyrotrophic Hormone ◽  
Thyroid Glands ◽  
Pre Treatment ◽  
Excess Iodide ◽  
Kidney Liver

ABSTRACT Lithium and excess iodide inhibit the release of thyroid hormone from preformed stores. We thus tested the hypothesis that this was due to an inhibition of thyroglobulin breakdown. Rats were pre-treated with propylthiouracil (PTU) for 3 weeks in order to deplete their thyroids of thyroglobulin. While the PTU was continued, lithium chloride (0.25 mEq./100 g weight) or potassium iodide (3 mg per rat) were injected every 12 h for 3 days. Thereafter the thyroglobulin content in thyroid gland homogenates was measured. PTU pre-treatment lowered the thyroglobulin content from 4.21 to 0.22 mg/100 mg gland. Lithium caused a marked re-accumulation of thyroglobulin to 0.60 mg/100 mg within 3 days. While iodide alone had only a borderline effect, it markedly potentiated the action of lithium and a combination of the two drugs increased the thyroglobulin content to 1.04 mg/100 mg. Thyroxine was injected into similarly pre-treated animals to suppress secretion of thyrotrophic hormone. This markedly inhibited the proteolysis of thyroglobulin and 1.3 mg/100 mg gland accumulated after 3 days. Excess iodide, given in addition to thyroxine, decreased the amount of thyroglobulin accumulated to 0.75 mg/100 mg gland. To study whether this could be explained by an inhibitory action of iodide on thyroglobulin biosynthesis, thyroid glands from animals treated with excess iodide were incubated in vitro in the presence of 0.2 mm iodide for 3 h. Iodide decreased the incorporation of radioactive leucine into total thyroidal protein and into thyroglobulin by 25 and 35 % respectively. Iodide did not inhibit protein synthesis in the kidney, liver or muscle tissue. Thus, large doses of iodide selectively inhibit thyroglobulin biosynthesis.

scholarly journals Protein synthesis in chloroplasts. Characteristics and products of protein synthesis in vitro in etioplasts and developing chloroplasts from pea leaves

1975 ◽  
Vol 146 (3) ◽  
pp. 675-685 ◽  
Author(s):  
S G Siddell ◽  
R J Ellis
Keyword(s):  
Energy Source ◽  
Protein Synthesis ◽  
Large Subunit ◽  
Sodium Dodecyl ◽  
Supernatant Fraction ◽  
Pisum Sativum L ◽  
Fraction I ◽  
Plastid Ribosomes

The function of plastid ribosomes in pea (Pisum sativum L.) was investigated by characterizing the products of protein synthesis in vitro in plastids isolated at different stages during the transition from etioplast to chloroplast. Etioplasts and plastids isolated after 24, 48 and 96h of greening in continuous white light, use added ATP to incorporate labelled amino acids into protein. Plastids isolated from greening leaves can also use light as the source of energy for protein synthesis. The labelled polypeptides synthesized in isolated plastids were analysed by electrophoresis in sodium dodecyl sulphate-ureapolyacrylamide gels. Six polypeptides are synthesized in etioplasts with ATP as energy source. Only one of these polypeptides is present in a 150 000g supernatant fraction. This polypeptide has been identified as the large subunit of Fraction I protein (3-phospho-D-glycerate carboxylyase EC 4.1.1.39) by comparing the tryptic ‘map’ of its L-(35S)methionine-labelled peptides with the tryptic ‘map’ of large subunit peptides from Fraction I labelled with L-(35S)methionine in vivo. The same gel pattern of six polypeptides is seen when plastids isolated from greening leaves are incubated with either added ATP or light as the energy source. However, the rates of synthesis of particular polypeptides are different in plastids isolated at different stages of the etioplast to chloroplast transition. The results support the idea that plastid ribosomes synthesize only a small number of proteins, and that the number and molecular weight of these proteins does not alter during the formation of chloroplasts from etioplasts.

Structure of the chloroplast and its DNA in chloromonadophycean algae

1981 ◽  
Vol 49 (1) ◽  
pp. 401-409
Author(s):  
A.W. Coleman ◽  
P. Heywood
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Membrane ◽  
Nuclear Envelope ◽  
Chloroplast Dna ◽  
Single Layer ◽  
Longitudinal Axis ◽  
Chloroplast Envelope ◽  
Large Numbers ◽  
Gonyostomum Semen ◽  
Chloroplast Stroma

The arrangement and ultrastructure of chloroplasts is described for the Chloromonadophycean algae gonyostomum semen Diesing and Vacuolaria virescens Cienkowsky. The chloroplasts are present in large numbers and are discoid structures approximately 3–4 micrometer in length by 2–3 micrometer in width. In Gonyostomum semen the chloroplasts form a single layer immediately interior to the cell membrane; frequently their longitudinal axis parallels the longitudinal axis of the cell. The chloroplasts in Vacuolaria virescens are more than I layer deep and do not appear to be preferentially oriented. In both organisms, chloroplast bands usually consist of 3 apposed thylakoids, although fusion and interconnections between adjacent bands frequently occur. External to the girdle band (the outermost thylakoids) is the chloroplast envelope. This is bounded by endoplasmic reticulum but there is no immediately apparent continuity between this endoplasmic reticulum and the nuclear envelope. Electron-dense spheres in the chloroplast stroma are thought to be lipid food reserve. Ring-shaped electron-translucent regions in the chloroplast contain chloroplast DNA. The DNA is distributed along this ring in an uneven fashion and, when stained, resembles a string of beads. Each plastid has I ring, and the ring is unbroken in the intact plastid.

The effects of D- and L-threo-chloramphenicol on the early development of the chick embryo

Development ◽  
1965 ◽  
Vol 13 (3) ◽  
pp. 341-356
Author(s):  
F. S. Billett ◽  
Rosalba Collini ◽  
Louie Hamilton
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Chick Embryo ◽  
Messenger Rna ◽  
Mammalian Cells ◽  
Animal Cells ◽  
Inhibit Protein Synthesis ◽  
Acid Complex ◽  
Amino Acid Complex ◽  
Bacterial Systems

In many bacterial systems chloramphenicol has been shown to inhibit protein synthesis (Hahn & Wisseman, 1951; Gale & Folkes, 1953). The precise mechanism of this inhibition is not clear, although the evidence suggests that the interaction of the soluble RNA-amino acid complex with the ribosomes is prevented because the attachment of the messenger RNA to the ribosomes is itself impaired (Lacks & Gros, 1959; Nathans & Lipman, 1961; Jardetsky & Julian, 1964; Julian & Jardetsky, 1964). In contrast to its effect on bacterial systems, chloramphenicol has been reported to have little or no action on the protein synthesis by cell-free extracts of mammalian cells (Rendi, 1959; Ehrenstein & Lipmann, 1961). A basis for this resistance has been proposed by Vazquez (1964), who finds that whereas bacterial ribosomes bind chloramphenicol, ribosomes from other organisms do not. Nevertheless, it cannot be stated with any confidence that chloramphenicol has no effect on the protein synthesis of animal cells.

scholarly journals An Investigation Into The Synergistic Relationship Between Lactoferrin And Azithromycin With Particular Reference To Periodontopathic Bacteria

2017 ◽  
Vol 16 (2) ◽  
Author(s):  
Juzaily Husain
Keyword(s):  
Protein Synthesis ◽  
Outer Membrane ◽  
Porphyromonas Gingivalis ◽  
Treatment Strategies ◽  
Antimicrobial Protein ◽  
Tannerella Forsythia ◽  
Iron Depletion ◽  
Test Strips ◽  
Agar Diffusion ◽  
Synergistic Relationship

Introduction: The development of treatment strategies for periodontitis that maximise the effectiveness of antibiotics is highly desirable. Azithromycin is proving to be an effective antibiotic for treatment of refractory periodontitis which works by binding to the outer membrane of Gramnegative bacteria and subsequently inhibits protein synthesis. Lactoferrin is a membrane-active host antimicrobial protein and so the objective of this study was to determine whether the effect of azithromycin (AZM) against example periodontopathogens (Porphyromonas gingivalis and Tannerella forsythia) could be potentiated by lactoferrin. Materials and Methods: Two strains of P. gingivalis and T. forsythia were exposed to lactoferrin (LF; up to 10 mg/ml) and AZM (up to 5 g/ml) for 0 -72 h. The MICs for AZM were established using E-Test strips and by agar diffusion. Susceptibility to LF and LF + AZM was evaluated using diffusion assays, with and without iron depletion. Results: The range of MIC values of AZM for P. gingivalis strains and T. forsythia was 0.16 - 0.63 µg/ml and 0.50 - 0.63 µg/ml, respectively. However, no inhibition was observed with iron saturated lactoferrin at any concentration or under iron depletion conditions nor was any effect observed on the AZM MIC by its presence. Conclusion(s): P. gingivalis and T. forsythia were inhibited by AZM but were not affected by LF and there was no synergism between AZM and LF.

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