GFP as a tool for the analysis of proteins in the flagellar basal apparatus ofChlamydomonas

2005 ◽  
Vol 61 (4) ◽  
pp. 189-200 ◽  
Author(s):  
Jutta Schoppmeier ◽  
Wolfgang Mages ◽  
Karl-Ferdinand Lechtreck
Keyword(s):  
Basal Apparatus

Ultrastructure of the basal body apparatus in epidermal cells of a sponge larva (Aplysilla SP: Demospongiae)

1992 ◽  
Vol 50 (1) ◽  
pp. 928-929
Author(s):  
R.L. Pinto ◽  
R.M. Woollacott
Keyword(s):  
Sodium Bicarbonate ◽  
Epoxy Resin ◽  
Basal Body ◽  
Phosphate Buffer ◽  
Similar Data ◽  
Basal Apparatus ◽  
Striated Rootlet ◽  
The Common ◽  
Basal Foot ◽  
Sexually Mature

The basal body and its associated rootlet are the organelles responsible for anchoring the flagellum or cilium in the cytoplasm. Structurally, the common denominators of the basal apparatus are the basal body, a basal foot from which microtubules or microfilaments emanate, and a striated rootlet. A study of the basal apparatus from cells of the epidermis of a sponge larva was initiated to provide a comparison with similar data on adult sponges.Sexually mature colonies of Aplysillasp were collected from Keehi Lagoon Marina, Honolulu, Hawaii. Larvae were fixed in 2.5% glutaraldehyde and 0.14 M NaCl in 0.2 M Millonig’s phosphate buffer (pH 7.4). Specimens were postfixed in 1% OsO4 in 1.25% sodium bicarbonate (pH 7.2) and embedded in epoxy resin. The larva ofAplysilla sp was previously described (as Dendrilla cactus) based on live observations and SEM by Woollacott and Hadfield.

scholarly journals Phosphorylation of nuclear and flagellar basal apparatus proteins during flagellar regeneration in Chlamydomonas reinhardtii

1993 ◽  
Vol 122 (4) ◽  
pp. 877-886 ◽  
Author(s):  
JD Harper ◽  
MA Sanders ◽  
JL Salisbury
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Transcriptional Activation ◽  
Kinase Inhibitor ◽  
Nuclear Periphery ◽  
Immunoblot Analysis ◽  
Basal Region ◽  
Western Immunoblot ◽  
Flagellar Regeneration ◽  
Basal Apparatus ◽  
Western Immunoblot Analysis

The antiphosphoprotein monoclonal antibody MPM-2 was used to investigate protein phosphorylation during flagellar regeneration in Chlamydomonas reinhardtii. MPM-2 recognizes a phosphorylated epitope and detects several Chlamydomonas proteins by Western immunoblot analysis. Two MPM-2 reactive proteins (34 and 90 kD) increase in Western immunoblot intensity after flagellar excision and decrease in intensity during flagellar regeneration. Immunofluorescence and immunogold labeling revealed MPM-2 staining within the nucleus, especially towards the nuclear periphery, the flagellar basal apparatus, and the nucleus-basal body connector after flagellar excision. Comparison of MPM-2 reactivity in wild-type cells and in the mutant bald-2, which lacks functional basal bodies, demonstrates that the 34-kD protein is localized in the nucleus and the 90-kD protein is localized in the flagellar basal region. MPM-2 reactivity is observed in cells competent for flagellar regeneration. However, when cells were treated with the kinase inhibitor, staurosporine, MPM-2 reactivity did not increase after flagellar excision and flagellar regeneration was impaired. These observations suggest that phosphorylation of the 34- and 90-kD proteins may be important for flagellar regrowth. Possible roles for phosphorylation in flagellar regeneration include transcriptional activation and transport of flagellar precursors to the base of the growing flagella.

Fine structural observations of Desulfovibrio desulfuricans

1973 ◽  
Vol 19 (6) ◽  
pp. 753-756
Author(s):  
Terrence M. Hammill ◽  
Geno J. Germano
Keyword(s):  
Electron Microscopy ◽  
Cell Division ◽  
Cell Envelope ◽  
Desulfovibrio Desulfuricans ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Ultrathin Sections ◽  
Basal Apparatus ◽  
Specialized Region ◽  
Whole Mounts

Glutaraldehyde-fixed, platinum-carbon-shadowed whole mounts, and ultrathin sections of glutaraldehyde-OsO4-fixed cells of Desulfovibrio desulfuricans were observed by electron microscopy. The preparations demonstrated a typical Vibrio form with a single polar flagellum. The cell envelope and the formation of external blebs were shown to be similar to other gram-negative bacteria. The protoplast, apparently devoid of mesosomes or other membranous structures, was densely packed with ribosomes and contained a fibrous nucleoid. A specialized region near the flagellar end of the cell was commonly observed and termed the basal apparatus. Cell division appeared to be by constriction.

scholarly journals Ultrastructural and immunohistochemical study of the basal apparatus of solitary cilia in the human oviduct epithelium

2002 ◽  
Vol 200 (1) ◽  
pp. 89-96 ◽  
Author(s):  
Haruo Hagiwara ◽  
Shinsuke Harada ◽  
Sakae Maeda ◽  
Takeo Aoki ◽  
Nobuo Ohwada ◽  
...  
Keyword(s):  
Immunohistochemical Study ◽  
Oviduct Epithelium ◽  
Basal Apparatus ◽  
Human Oviduct

The control of anthozoan cilia by the basal apparatus

1982 ◽  
Vol 14 (4) ◽  
pp. 607-620 ◽  
Author(s):  
M.C. Holley
Keyword(s):  
Basal Apparatus

scholarly journals Calcium control of ciliary arrest in mussel gill cells.

1978 ◽  
Vol 79 (1) ◽  
pp. 110-120 ◽  
Author(s):  
M F Walter ◽  
P Satir
Keyword(s):  
Sodium Phosphate ◽  
Freshwater Mussels ◽  
Ciliated Cell ◽  
Cell Types ◽  
Gill Epithelium ◽  
Ciliated Cells ◽  
Ciliary Membrane ◽  
Gill Cells ◽  
Basal Apparatus ◽  
Triton X

After several hours in 20 mM sodium phosphate and 40 mM KCI (pH 7.4) or similar simple solutions, ciliated cells exfoliate en masse from stripped gill epithelium of freshwater mussels, e.g., Elliptio complanatus. Three types of ciliated cells--lateral (L), laterofrontal (LF), and frontal (F)--can be distiniguished and counted separately in the suspensions. About one-half of the cells of each type remain motile. Motility is unaffected by addition of 10(-5) M A23187 or 10(-2) M Ca+2 added separately, but when ionophore and Ca+2 are added together, ciliary beat is largely arrested. Treatment of the cells with Triton X-100 (Rohm & Haas Co., Philadelphia, Pa.) results in a total loss of motility as the ciliary membrane becomes disrupted. Such models can be reactivated by addition of ATP and Mg+2. All ciliated cell types are reactivated to about the same extent. At least 80% of the activity of the untreated preparation returns. Ca+2-EGTA buffers added to the reactivating solutions permit titration of free Ca+2 concentration vs. percent motility. Activity is unchanged for all cell types at Ca+2 less than 10(-7) M; at 10(-6) Ca+2, L cilia of all cell types are arrested differentially, whereas at Ca+2 greater than 10(-4) M most cilia of all cell types are arrested. We conclude: (a) that increasing cytoplasmic Ca+2 is directly responsible for ciliary arrest, (b) that the readily reversible physiological arrest response of the L cilia in the intact gill is caused by a rise in free Ca+2 in narrow limits from ca. 5 x 10(-7) M to ca. 8 x 10(-7) M, and (c) that the site which is sensitive to Ca+2 is part of the ciliary axoneme or the basal apparatus.

Basal apparatus behaviour during cellular division (sporulation) in the coccoid green algaChlorosarcina

PROTOPLASMA ◽  
1990 ◽  
Vol 155 (1-3) ◽  
pp. 66-75 ◽  
Author(s):  
H. J. Sluiman ◽  
P. C. J. Blommers
Keyword(s):  
Cellular Division ◽  
Basal Apparatus
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