scholarly journals THE FORMATION OF BASAL BODIES (CENTRIOLES) IN THE RHESUS MONKEY OVIDUCT

1971 ◽  
Vol 50 (1) ◽  
pp. 10-34 ◽  
Author(s):  
Richard G. W. Anderson ◽  
Robert M. Brenner
Keyword(s):  
Rhesus Monkey ◽  
Basal Body ◽  
Wall Material ◽  
Basal Bodies ◽  
Major Pathway ◽  
Tubule Formation ◽  
Body Formation ◽  
Body Production ◽  
Basal Foot ◽  
Section Analysis

Basal body replication during estrogen-driven ciliogenesis in the rhesus monkey (Macaca mulatta) oviduct has been studied by stereomicroscopy, rotation photography, and serial section analysis. Two pathways for basal body production are described: acentriolar basal body formation (major pathway) where procentrioles are generated from a spherical aggregate of fibers; and centriolar basal body formation, where procentrioles are generated by the diplosomal centrioles. In both pathways, the first step in procentriole formation is the arrangement of a fibrous granule precursor into an annulus. A cartwheel structure, present within the lumen of the annulus, is composed of a central cylinder with a core, spoke components, and anchor filaments. Tubule formation consists of an initiation and a growth phase. The A tubule of each triplet set first forms within the wall material of the annulus in juxtaposition to a spoke of the cartwheel. After all nine A tubules are initiated, B and C tubules begin to form. The initiation of all three tubules occurs sequentially around the procentriole. Simultaneous with tubule initiation is a nonsequential growth of each tubule. The tubules lengthen and the procentriole is complete when it is about 200 mµ long. The procentriole increases in length and diameter during its maturation into a basal body. The addition of a basal foot, nine alar sheets, and a rootlet completes the maturation process. Fibrous granules are also closely associated with the formation of these basal body accessory structures.

scholarly journals Sfr1, a Tetrahymena thermophila Sfi1 Repeat Protein, Modulates the Production of Cortical Row Basal Bodies

mSphere ◽  
2016 ◽  
Vol 1 (6) ◽  
Author(s):  
Westley Heydeck ◽  
Alexander J. Stemm-Wolf ◽  
Janin Knop ◽  
Christina C. Poh ◽  
Mark Winey
Keyword(s):  
Basal Body ◽  
Binding Proteins ◽  
Tetrahymena Thermophila ◽  
Binding Protein ◽  
Extensive Study ◽  
Basal Bodies ◽  
Content Type ◽  
Inhibitory Role ◽  
Body Production

ABSTRACT Basal bodies and centrioles are structurally similar and, when rendered dysfunctional as a result of improper assembly or maintenance, are associated with human diseases. Centrins are conserved and abundant components of both structures whose basal body and centriolar functions remain incompletely understood. Despite the extensive study of centrins in Tetrahymena thermophila, little is known about how centrin-binding proteins contribute to centrin’s roles in basal body assembly, stability, and orientation. The sole previous study of the large centrin-binding protein family in Tetrahymena revealed a role for Sfr13 in the stabilization and separation of basal bodies. In this study, we found that Sfr1 localizes to all Tetrahymena basal bodies and complete genetic deletion of SFR1 leads to overproduction of basal bodies. The uncovered inhibitory role of Sfr1 in basal body production suggests that centrin-binding proteins, as well as centrins, may influence basal body number both positively and negatively. Basal bodies are essential microtubule-based structures that template, anchor, and orient cilia at the cell surface. Cilia act primarily in the generation of directional fluid flow and sensory reception, both of which are utilized for a broad spectrum of cellular processes. Although basal bodies contribute to vital cell functions, the molecular contributors of their assembly and maintenance are poorly understood. Previous studies of the ciliate Tetrahymena thermophila revealed important roles for two centrin family members in basal body assembly, separation of new basal bodies, and stability. Here, we characterize the basal body function of a centrin-binding protein, Sfr1, in Tetrahymena. Sfr1 is part of a large family of 13 proteins in Tetrahymena that contain Sfi1 repeats (SFRs), a motif originally identified in Saccharomyces cerevisiae Sfi1 that binds centrin. Sfr1 is the only SFR protein in Tetrahymena that localizes to all cortical row and oral apparatus basal bodies. In addition, Sfr1 resides predominantly at the microtubule scaffold from the proximal cartwheel to the distal transition zone. Complete genomic knockout of SFR1 (sfr1Δ) causes a significant increase in both cortical row basal body density and the number of cortical rows, contributing to an overall overproduction of basal bodies. Reintroduction of Sfr1 into sfr1Δ mutant cells leads to a marked reduction of cortical row basal body density and the total number of cortical row basal bodies. Therefore, Sfr1 directly modulates cortical row basal body production. This study reveals an inhibitory role for Sfr1, and potentially centrins, in Tetrahymena basal body production. IMPORTANCE Basal bodies and centrioles are structurally similar and, when rendered dysfunctional as a result of improper assembly or maintenance, are associated with human diseases. Centrins are conserved and abundant components of both structures whose basal body and centriolar functions remain incompletely understood. Despite the extensive study of centrins in Tetrahymena thermophila, little is known about how centrin-binding proteins contribute to centrin’s roles in basal body assembly, stability, and orientation. The sole previous study of the large centrin-binding protein family in Tetrahymena revealed a role for Sfr13 in the stabilization and separation of basal bodies. In this study, we found that Sfr1 localizes to all Tetrahymena basal bodies and complete genetic deletion of SFR1 leads to overproduction of basal bodies. The uncovered inhibitory role of Sfr1 in basal body production suggests that centrin-binding proteins, as well as centrins, may influence basal body number both positively and negatively.

scholarly journals Mcidas mutant mice reveal a two-step process for the specification and differentiation of multiciliated cells in mammals

2018 ◽  
Author(s):  
Hao Lu ◽  
Priyanka Anujan ◽  
Feng Zhou ◽  
Yiliu Zhang ◽  
Yan Ling Chong ◽  
...  
Keyword(s):  
Basal Body ◽  
Target Genes ◽  
Initial Step ◽  
Mutant Mice ◽  
Respiratory Disorder ◽  
Basal Bodies ◽  
Cell Cycle Regulators ◽  
Multiciliated Cells ◽  
Motile Cilia ◽  
Body Production

ABSTRACTMotile cilia on multiciliated cells (MCCs) function in fluid clearance over epithelia. Studies with Xenopus embryos and patients with the congenital respiratory disorder reduced generation of multiple motile cilia, have implicated the nuclear protein MCIDAS (MCI), in the transcriptional regulation of MCC specification and differentiation. Recently, a paralogous protein, GMNC, was also shown to be required for MCC formation. Surprisingly, and in contrast to the presently held view, we find that Mci mutant mice can specify MCC precursors. However, these precursors cannot produce multiple basal bodies, and mature into single ciliated cells. We show that MCI is required specifically to induce deuterosome pathway components for the production of multiple basal bodies. Moreover, GMNC and MCI associate differentially with the cell-cycle regulators E2F4 and E2F5, which enables them to activate distinct sets of target genes (ciliary transcription factor genes versus genes for basal body generation). Our data establish a previously unrecognized two-step model for MCC development: GMNC functions in the initial step for MCC precursor specification. GMNC induces Mci expression, which then drives the second step of basal body production for multiciliation.SUMMARY STATEMENTWe show how two GEMININ family proteins function in mammalian multiciliated cell development: GMNC regulates precursor specification and MCIDAS induces multiple basal body formation for multiciliation.

scholarly journals THE RELATIONSHIP BETWEEN THE FINE STRUCTURE AND DIRECTION OF BEAT IN GILL CILIA OF A LAMELLIBRANCH MOLLUSC

1961 ◽  
Vol 11 (1) ◽  
pp. 179-205 ◽  
Author(s):  
I. R. Gibbons
Keyword(s):  
Fine Structure ◽  
Cell Surface ◽  
Basal Body ◽  
Transitional Region ◽  
Basal Bodies ◽  
Conical Structure ◽  
The Relationship ◽  
Basal Foot ◽  
Different Levels ◽  
Outer Fiber

This paper describes the fine structure and its relationship to the direction of beat in four types of cilia on the gill of the fresh-water mussel Anodonta cataracta. The cilia contain nine outer, nine secondary, and two central fibers, such as have been described previously in other material. Each outer fiber is a doublet with one subfiber bearing arms. One particular pair of outer fibers (numbers 5 and 6) are joined together by a bridge. The two central fibers are enclosed by a central sheath; also present in this region is a single, small mid-fiber. The different groups of fibers are connected together by radial links that extend from the outer to the secondary fibers, and from the secondary fibers to the central sheath. The basal body consists of a cylinder of nine triplet fibers. Projecting from it on one side is a dense conical structure called the basal foot. The cylinder of outer fibers continues from the basal body into the cilium, passing through a complex transitional region in which five distinct changes of structure occur at different levels. There are two sets of fibers associated with the basal bodies: a pair of striated rootlets that extends from each basal body down into the cell, and a system of fine tubular fibers that runs parallel to the cell surface. The relationship between fine structure and direction of beat is the same in all four types of cilia examined. The plane of beat is perpendicular to the plane of the central fibers, with the effective stroke toward the bridge between outer fibers 5 and 6, and toward the foot on the basal body.

scholarly journals Identification of contractile proteins in basal bodies of ciliated tracheal epithelial cells.

1980 ◽  
Vol 28 (11) ◽  
pp. 1189-1197 ◽  
Author(s):  
R E Gordon ◽  
B P Lane ◽  
F Miller
Keyword(s):  
Basal Body ◽  
Contractile Function ◽  
Ultrastructural Localization ◽  
Immunoperoxidase Technique ◽  
Basal Bodies ◽  
Tracheal Epithelial Cells ◽  
Tracheal Epithelial ◽  
Indirect Immunoperoxidase ◽  
Basal Foot ◽  
Basal Density

To determine the molecular composition of the components of basal bodies and the interbasal body apparatus of ciliated cells in rat tracheal epithelium, we used rabbit anti-actin, anti-alpha-actinin, anti-tropomyosin, and anti-myosin as primary antisera applied to the tissue in an indirect immunoperoxidase technique. The antisera was proven to be monospecific by elution of antibody after affinity chromatography. Sheep anti-rabbit immunoglobulin Fab fragments coupled to peroxidase were used for ultrastructural localization of the bound rabbit antibody. Antibodies against alpha-actinin were demonstrated around peripheral microtubules of cilia and linking these microtubules to central doublet and plasma membrane. Alpha-actinin was also shown in the basal foot processes. Anti-actin antibodies were associated with microtubules of the cilium and basal bodies, except in the region of the ciliary necklace. The antibodies directed against actin also had affinity for rootlets, basal foot processes, and communications between basal bodies and foot processes. Both anti-myosin and anti-tropomyosin antibodies were localized to part of the region of the constriction of the cilium, to the central basal density and the outer surfaces of basal body microtubules, and to the basal foot processes together with their communications to the basal body. The data suggest active contractile function of basal bodies.

scholarly journals Biochemical and cytochemical evidence for ATPase activity in basal bodies isolated from oviduct.

1977 ◽  
Vol 74 (2) ◽  
pp. 547-560 ◽  
Author(s):  
R G Anderson
Keyword(s):  
Enzyme Activity ◽  
Atpase Activity ◽  
Basal Body ◽  
Divalent Cation ◽  
Specific Activity ◽  
Basal Bodies ◽  
Ph Optimum ◽  
Outer Portion ◽  
Chicken Oviduct ◽  
Basal Foot

Biochemical and cytochemical techniques were used to determine whether oviduct basal bodies have ATPase activity. All studies were carried out on basal bodies isolated and purified from the chicken oviduct. These preparations contained structurally intact basal bodies with basal feet, rootlet, and alar sheet accessory structures. Whereas the specific activity of the basal body ATPase in 2 mM Ca++ or 2 mM Mg++, 1 mM ATP, pH 8.0, averaged 0.04 mumol Pi/min per mg protein, higher concentrations of either cation inhibited the enzyme activity. Furthermore, the pH optimum for this reaction was pH 8.5. In comparison, the ATPase activity in cilia purified and measured under conditions identical to those for determining the basal body ATPase activity averaged 0.07 mumol Pi/min per mg protein. However, the activity increased at higher concentrations of divalent cation, and the pH optimum was pH 10.0. By cytochemical procedures for localizing ATPase activity, ATP-dependent reaction product in isolated basal bodies was found to be confined to: (a) the cross-striations of the rootlet; (b) the outer portion of the basal foot; (c) the alar sheets; and (d) the triplet microtubules. It is concluded that basal bodiesve an intrinsic ATPase activity that, by a variety of criteria, can be distinguished from the ATPase activity found in cilia.

scholarly journals The molecular dynamics of subdistal appendages in multi-ciliated cells

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Hyunchul Ryu ◽  
Haeryung Lee ◽  
Jiyeon Lee ◽  
Hyuna Noh ◽  
Miram Shin ◽  
...  
Keyword(s):  
Basal Body ◽  
Ependymal Cells ◽  
Basal Bodies ◽  
Ciliary Beating ◽  
Sam Domain ◽  
Adult Mice ◽  
Region I ◽  
Evolutionarily Conserved ◽  
Basal Foot

AbstractThe motile cilia of ependymal cells coordinate their beats to facilitate a forceful and directed flow of cerebrospinal fluid (CSF). Each cilium originates from a basal body with a basal foot protruding from one side. A uniform alignment of these basal feet is crucial for the coordination of ciliary beating. The process by which the basal foot originates from subdistal appendages of the basal body, however, is unresolved. Here, we show FGFR1 Oncogene Partner (FOP) is a useful marker for delineating the transformation of a circular, unpolarized subdistal appendage into a polarized structure with a basal foot. Ankyrin repeat and SAM domain-containing protein 1A (ANKS1A) interacts with FOP to assemble region I of the basal foot. Importantly, disruption of ANKS1A reduces the size of region I. This produces an unstable basal foot, which disrupts rotational polarity and the coordinated beating of cilia in young adult mice. ANKS1A deficiency also leads to severe degeneration of the basal foot in aged mice and the detachment of cilia from their basal bodies. This role of ANKS1A in the polarization of the basal foot is evolutionarily conserved in vertebrates. Thus, ANKS1A regulates FOP to build and maintain the polarity of subdistal appendages.

scholarly journals Evidence that the Synchronized Production of New Basal Bodies is not Associated with Dna Synthesis in Stentor Coeruleus

1972 ◽  
Vol 11 (2) ◽  
pp. 621-637
Author(s):  
K. B. YOUNGER ◽  
S. BANERJEE ◽  
J. K. KELLEHER ◽  
M. WINSTON ◽  
LYNN MARGULIS
Keyword(s):  
Dna Synthesis ◽  
Ethidium Bromide ◽  
Basal Body ◽  
Actinomycin D ◽  
Thymidine Incorporation ◽  
Basal Bodies ◽  
Rna And Protein Synthesis ◽  
Stentor Coeruleus ◽  
Body Production ◽  
Dna Synthesis Inhibitors

Stentors were induced to produce synchronously thousands of new ciliated oral membranellar band basal bodies in less than 3 h. DNA synthesis does not accompany this process, as determined by [3H]thymidine incorporation into isolated bands and by sensitivity to DNA synthesis inhibitors (mitomycin C, ethidium bromide, cytosine arabinoside and hydroxyurea). Yet DNA could be detected in the cortex and the band at basal body sites by autoradiography. Since [3H]thymidine incorporation into membranellar band was eliminated in concentrations of ethidium bromide that had no effect on basal body formation, the previous reports of ciliate kinetosomal (basal body) DNA are interpreted as due to mitochondrial contamination. Specific cortical patterns of DNA that could have been easily misinterpreted as basal body-related were especially apparent in autoradiographs using [3H]actinomycin D as a ‘stain’. In no experiment involving induced basal body regeneration could evidence be found for a correlation between new basal body production and DNA synthesis; RNA and protein synthesis correlated with basal body and cilia regeneration were, however, easily detected by the same techniques. We concluded that there is no evidence that basal body DNA synthesis is required for new basal body production.

scholarly journals Basal Body Components Exhibit Differential Protein Dynamics during Nascent Basal Body Assembly

2009 ◽  
Vol 20 (3) ◽  
pp. 904-914 ◽  
Author(s):  
Chad G. Pearson ◽  
Thomas H. Giddings ◽  
Mark Winey
Keyword(s):  
Basal Body ◽  
Tetrahymena Thermophila ◽  
Light And Electron Microscopy ◽  
Protein Assembly ◽  
Basal Bodies ◽  
Body Formation ◽  
Unique Protein ◽  
Body Components ◽  
And Function ◽  
Stable Populations

Basal bodies organize cilia that are responsible for both mechanical beating and sensation. Nascent basal body assembly follows a series of well characterized morphological events; however, the proteins and their assembly dynamics for new basal body formation and function are not well understood. High-resolution light and electron microscopy studies were performed in Tetrahymena thermophila to determine how proteins assemble into the structure. We identify unique dynamics at basal bodies for each of the four proteins analyzed (α-tubulin, Spag6, centrin, and Sas6a). α-Tubulin incorporates only during new basal body assembly, Spag6 continuously exchanges at basal bodies, and centrin and Sas6a exhibit both of these patterns. Centrin loads and exchanges at the basal body distal end and stably incorporates during new basal body assembly at the nascent site of assembly and the microtubule cylinder. Conversely, both dynamic and stable populations of Sas6a are found only at a single site, the cartwheel. The bimodal dynamics found for centrin and Sas6a reveal unique protein assembly mechanisms at basal bodies that may reflect novel functions for these important basal body and centriolar proteins.

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.

Ciliary coordination in newt lung cells requires microtubule-based linkages between basal bodies: A correlative light and EM study

1992 ◽  
Vol 50 (1) ◽  
pp. 570-571
Author(s):  
Robert Hard ◽  
Gerald Rupp ◽  
Matthew L. Withiam-Leitch ◽  
Lisa Cardamone
Keyword(s):  
Basal Body ◽  
Untreated Control ◽  
Beat Frequency ◽  
Primary Cultures ◽  
Living Cells ◽  
Power Stroke ◽  
Ultrastructural Changes ◽  
Lung Cells ◽  
Basal Bodies ◽  
Ciliated Cells

In a coordinated field of beating cilia, the direction of the power stroke is correlated with the orientation of basal body appendages, called basal feet. In newt lung ciliated cells, adjacent basal feet are interconnected by cold-stable microtubules (basal MTs). In the present study, we investigate the hypothesis that these basal MTs stabilize ciliary distribution and alignment. To accomplish this, newt lung primary cultures were treated with the microtubule disrupting agent, Colcemid. In newt lung cultures, cilia normally disperse in a characteristic fashion as the mucociliary epithelium migrates from the tissue explant. Four arbitrary, but progressive stages of dispersion were defined and used to monitor this redistribution process. Ciliaiy beat frequency, coordination, and dispersion were assessed for 91 hrs in untreated (control) and treated cultures. When compared to controls, cilia dispersed more rapidly and ciliary coordination decreased markedly in cultures treated with Colcemid (2 mM). Correlative LM/EM was used to assess whether these effects of Colcemid were coupled to ultrastructural changes. Living cells were defined as having coordinated or uncoordinated cilia and then were processed for transmission EM.

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