scholarly journals Functional reconstitution of Chlamydomonas outer dynein arms from alpha-beta and gamma subunits: requirement of a third factor.

1994 ◽  
Vol 126 (3) ◽  
pp. 737-745 ◽  
Author(s):  
S Takada ◽  
R Kamiya
Keyword(s):  
Cross Section ◽  
Cross Sections ◽  
Attachment Site ◽  
The Other ◽  
Wild Type ◽  
Heavy Chains ◽  
Sds Page ◽  
Gamma Subunits ◽  
Dynein Arms ◽  
Alpha Beta

The outer dynein arm of Chlamydomonas flagella, when isolated under Mg(2+)-free conditions, tends to dissociate into an 11 to 12S particle (12S dynein) containing the gamma heavy chain and a 21S particle (called 18S dynein) containing the alpha and beta heavy chains. We show here that functional outer arms can be reconstituted by the addition of 12S and 18S dyneins to the axonemes of the outer armless mutants oda1-oda6. A third factor that sediments at integral 7S is required for efficient reconstitution of the outer arms on the axonemes of oda1 and oda3. However, this factor is not necessary for reconstitution on the axonemes of oda2, oda4, oda5, and oda6. SDS-PAGE analysis indicates that the axonemes of the former two mutants lack a integral of 70-kD polypeptide that is present in those of the other mutants as well as in the 7S fraction from the wild-type extract. Furthermore, electron micrographs of axonemal cross sections revealed that the latter four mutants, but not oda1 or oda3, have small pointed structures on the outer doublets, at a position in cross section where outer arms normally occur. We suggest that the 7S factor constitutes the pointed structure on the outer doublets and facilitates attachment of the outer arm. The discovery of this structure raises a new question as to how the attachment site for the outer arm dynein is determined within the axoneme.

scholarly journals Two types of Chlamydomonas flagellar mutants missing different components of inner-arm dynein.

1991 ◽  
Vol 112 (3) ◽  
pp. 441-447 ◽  
Author(s):  
R Kamiya ◽  
E Kurimoto ◽  
E Muto
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Cross Section ◽  
Double Mutant ◽  
The Other ◽  
Flagellar Motility ◽  
Wild Type ◽  
Single Group ◽  
Heavy Chains ◽  
Section Electron ◽  
Dynein Arms

Two types of Chlamydomonas reinhardtii flagellar mutants (idaA and idaB) lacking partial components of the inner-arm dynein were isolated by screening mutations that produce paralyzed phenotypes when present in a mutant missing outer-arm dynein. Of the currently identified three inner-arm subspecies I1, I2, and I3, each containing two heterologous heavy chains (Piperno, G., Z. Ramanis, E. F. Smith, and W. S. Sale. 1990. J. Cell Biol. 110:379-389), idaA and idaB lacked I1 and I2, respectively. The 13 idA isolates comprised three genetically different groups (ida1, ida2, ida3) and the two idaB isolates comprised a single group (ida4). In averaged cross-section electron micrographs, inner dynein arms in wild-type axonemes appeared to have two projections pointing to discrete directions. In ida1-3 and ida4 axonemes, on the other hand, either one of them was missing or greatly diminished. Both projections were weak in the double mutant ida1-3 x ida4. These observations suggest that the inner dynein arms in Chlamydomonas axonemes are aligned not in a single straight row, but in a staggered row or two discrete rows. Both ida1-3 and ida4 swam at reduced speed. Thus, the inner-arm subspecies missing in these mutants are not necessary for flagellar motility. However, the double mutants ida1-3 x ida4 were nonmotile, suggesting that axonemes with significant defects in inner arms cannot function. The inner-arm dynein should be important for the generation of axonemal beating.

scholarly journals A Chlamydomonas outer arm dynein mutant with a truncated beta heavy chain

1993 ◽  
Vol 122 (3) ◽  
pp. 653-661 ◽  
Author(s):  
H Sakakibara ◽  
S Takada ◽  
SM King ◽  
GB Witman ◽  
R Kamiya
Keyword(s):  
Cross Sections ◽  
Heavy Chain ◽  
Swimming Velocity ◽  
Wild Type ◽  
Terminal Part ◽  
Electron Microscopic ◽  
Heavy Chains ◽  
Dynein Arms ◽  
Alpha Beta ◽  
Arm Function

A new allele of the Chlamydomonas oda4 flagellar mutant (oda4-s7) possessing abnormal outer dynein arms was isolated. Unlike the previously described oda4 axoneme lacking all three (alpha, beta, and gamma) outer-arm dynein heavy chains, the oda4-s7 axoneme contains the alpha and gamma heavy chains and a novel peptide with a molecular mass of approximately 160 kD. The peptide reacts with a mAb (18 beta B) that recognizes an epitope on the NH2-terminal part of the beta heavy chain. These observations indicate that this mutant has a truncated beta heavy chain, and that the NH2-terminal part of the beta heavy chain is important for the stable assembly of the outer arms. In averaged electron microscopic images of outer arms from cross sections of axonemes, the mutant outer arm lacks its mid-portion, producing a forked appearance. Together with our previous finding that the mutant oda11 lacks the alpha heavy chain and the outermost portion of the arm (Sakakibara, H., D. R. Mitchell, and R. Kamiya. 1991. J. Cell Biol. 113:615-622), this result defines the approximate locations of the three outer arm heavy chains in the axonemal cross section. The swimming velocity of oda4-s7 is 65 +/- 8 microns/s, close to that of oda4 which lacks the entire outer arm (62 +/- 8 microns/s) but significantly lower than the velocities of wild type (194 +/- 23 microns/s) and oda11 (119 +/- 17 microns/s). Thus, the lack of the beta heavy chain impairs outer-arm function more seriously than does the lack of the alpha heavy chain, suggesting that the alpha and beta chains play different roles in outer arm function.

Electron Irradiation Effects in Polyoxymethylene Crystals Grown Inside Trioxane Crystals

1971 ◽  
Vol 29 ◽  
pp. 78-79
Author(s):  
J. P. Colson ◽  
D. H. Reneker
Keyword(s):  
Cross Section ◽  
Cross Sections ◽  
Detailed Examination ◽  
The Other ◽  
Electron Micrograph ◽  
Irradiation Effects ◽  
Threefold Axis ◽  
Typical Sample ◽  
Polymer Crystals ◽  
Chain Axis

Polyoxymethylene (POM) crystals grow inside trioxane crystals which have been irradiated and heated to a temperature slightly below their melting point. Figure 1 shows a low magnification electron micrograph of a group of such POM crystals. Detailed examination at higher magnification showed that three distinct types of POM crystals grew in a typical sample. The three types of POM crystals were distinguished by the direction that the polymer chain axis in each crystal made with respect to the threefold axis of the trioxane crystal. These polyoxymethylene crystals were described previously.At low magnifications the three types of polymer crystals appeared as slender rods. One type had a hexagonal cross section and the other two types had rectangular cross sections, that is, they were ribbonlike.

scholarly journals Chlamydomonas WDR92 in association with R2TP-like complex and multiple DNAAFs to regulate ciliary dynein preassembly

2018 ◽  
Vol 11 (9) ◽  
pp. 770-780 ◽  
Author(s):  
Guang Liu ◽  
Limei Wang ◽  
Junmin Pan
Keyword(s):  
Mass Spectrometry ◽  
Insertional Mutagenesis ◽  
The Other ◽  
Cytoplasmic Protein ◽  
Flagellar Motility ◽  
Heavy Chains ◽  
The Third ◽  
Axonemal Dynein ◽  
Dynein Arms ◽  
Dna Insertional Mutagenesis

Abstract The motility of cilia or eukaryotic flagella is powered by the axonemal dyneins, which are preassembled in the cytoplasm by proteins termed dynein arm assembly factors (DNAAFs) before being transported to and assembled on the ciliary axoneme. Here, we characterize the function of WDR92 in Chlamydomonas. Loss of WDR92, a cytoplasmic protein, in a mutant wdr92 generated by DNA insertional mutagenesis resulted in aflagellate cells or cells with stumpy or short flagella, disappearance of axonemal dynein arms, and diminishment of dynein arm heavy chains in the cytoplasm, suggesting that WDR92 is a DNAAF. Immunoprecipitation of WDR92 followed by mass spectrometry identified inner dynein arm heavy chains and multiple DNAAFs including RuvBL1, RPAP3, MOT48, ODA7, and DYX1C. The PIH1 domain-containing protein MOT48 formed a R2TP-like complex with RuvBL1/2 and RPAP3, while PF13, another PIH1 domain-containing protein with function in dynein preassembly, did not. Interestingly, the third PIH1 domain-containing protein TWI1 was not related to flagellar motility. WDR92 physically interacted with the R2TP-like complex and the other identified DNNAFs. Our data suggest that WDR92 functions in association with the HSP90 co-chaperone R2TP-like complex as well as linking other DNAAFs in dynein preassembly.

The Brittleness of Ebonite

1937 ◽  
Vol 10 (4) ◽  
pp. 778-786
Author(s):  
R. Ariano
Keyword(s):  
Mechanical Properties ◽  
Cross Section ◽  
Cross Sections ◽  
Test Specimen ◽  
The State ◽  
The Other ◽  
Appreciable Effect ◽  
Considerable Influence ◽  
Minimum Depth ◽  
The Moment

Abstract The results of tests of the brittleness of ebonite are described. Resilience is influenced chiefly by the moment of inertia of the cross section of the test-specimen, but it seems also to be affected by the form of the specimen. The state of vulcanization has considerable influence on these mechanical properties within the undercured range, but with thorough vulcanization the state of cure plays no appreciable part. Notching of test-specimens is not of great importance. It diminishes the resilience, but when the tests are compared on a basis of equal moments of inertia of the resistant cross sections, this diminution becomes inappreciable in the case of brittle ebonites. On the other hand, the shape of the notch in ebonites containing no loading ingredients does influence the resilience. With V-shaped notches, the depth of the notch and its angle of aperture influence considerably the resilience of this latter type of ebonite, and notches of minimum depth are sufficient to have an appreciable effect.

Proton-proton scattering at the C. E. R. N. Intersecting Storage Rings

1973 ◽  
Vol 335 (1603) ◽  
pp. 431-452 ◽  
Keyword(s):  
Cross Section ◽  
Cross Sections ◽  
High Energy ◽  
Storage Rings ◽  
The Other ◽  
Proton Scattering ◽  
High Energy Proton ◽  
Proton Proton ◽  
Total Cross Sections ◽  
Energy Proton

The main features of the C. E. R. N. Intersecting Storage Rings (I. S. R.) are reviewed, together with results obtained in 1971 and 1972 on elastic scattering and total cross-sections. The main result is a 10% increase of the total proton-proton cross-section in the I. S. R. energy range. The simplest picture of high energy proton-proton scattering which emerges from this and the other data, is briefly discussed.

scholarly journals Components of a "dynein regulatory complex" are located at the junction between the radial spokes and the dynein arms in Chlamydomonas flagella.

1994 ◽  
Vol 127 (5) ◽  
pp. 1311-1325 ◽  
Author(s):  
L C Gardner ◽  
E O'Toole ◽  
C A Perrone ◽  
T Giddings ◽  
M E Porter
Keyword(s):  
Liquid Chromatography ◽  
Cross Sections ◽  
Close Association ◽  
Longitudinal Section ◽  
Radial Spoke ◽  
Sds Page ◽  
Radial Spokes ◽  
Regulatory Complex ◽  
Dynein Arms ◽  
The Relationship

Previous studies of flagellar mutants have identified six axonemal polypeptides as components of a "dynein regulatory complex" (DRC). The DRC is though to coordinate the activity of the multiple flagellar dyneins, but its location within the axoneme has been unknown (Huang et al., 1982; Piperno et al., 1992). We have used improved chromatographic procedures (Kagami and Kamiya, 1992) and computer averaging of EM images (Mastronarde et al., 1992) to analyze the relationship between the DRC and the dynein arms. Our results suggest that some of the DRC components are located at the base of the second radial spoke in close association with the inner dynein arms. (a) Averages of axoneme cross-sections indicate that inner arm structures are significantly reduced in three DRC mutants (pf3 < pf2 < sup-pf-3 < wt). (b) These defects are more pronounced in distal/medial regions of the axoneme than in proximal regions. (c) Analysis of flagellar extracts by fast protein liquid chromatography and SDS-PAGE indicates that a specific dynein I2 isoform is missing in pf3 and reduced in pf2 and sup-pf-3. Comparison with ida4 and pf3ida4 extracts reveals that this isoform differs from those missing in ida4. (d) When viewed in longitudinal section, all three DRC mutants lack a crescent-shaped density above the second radial spoke, and pf3 axonemes lack additional structures adjacent to the crescent. We propose that the crescent corresponds in part to the location of the DRC, and that this structure is also directly associated with a subset of the inner dynein arms. This position is appropriate for a complex that is thought to mediate signals between the radial spokes and the dynein arms.

scholarly journals A study by a double-refraction method of the development of turbulence in a long circular tube

1947 ◽  
Vol 192 (1028) ◽  
pp. 32-44 ◽  
Keyword(s):  
Reynolds Number ◽  
Weak Solution ◽  
Laminar Flow ◽  
Cross Section ◽  
Cross Sections ◽  
Circular Tube ◽  
Glass Tube ◽  
The Other ◽  
Double Refraction ◽  
Refraction Method

A streaming double-refraction method was employed to examine the flow in a long glass tube of a very weak solution of benzopurpurin in water. Two kinds of turbulent entry were used: with one, laminar flow at a Reynolds number of about 1900 was observed at cross-sections more than 120 diameters from the entry; with the other the corresponding distance was 90 diameters. The nature of the breakdown of laminar flow at a cross-section was found to depend upon the kind of entry and upon the distance of the cross-section from the inlet. The development of complete turbulence at various cross-sections was also investigated.

scholarly journals Curved composite beam with interlayer slip loaded by radial load

2015 ◽  
Vol 2 (1) ◽  
Author(s):  
István Ecsedi ◽  
Ákos József Lengyel
Keyword(s):  
Linear Relationship ◽  
Cross Section ◽  
Cross Sections ◽  
Composite Beam ◽  
The Other ◽  
Radial Load ◽  
Rigid Plate ◽  
Shear Connection ◽  
First Case ◽  
Interlayer Slip

AbstractElastic two-layer curved composite beam with partial shear interaction is considered. It is assumed that each curved layer separately follows the Euler-Bernoulli hypothesis and the load slip relation for the flexible shear connection is a linear relationship. The curved composite beam at one of the end cross sections is fixed and the other end cross section is subjected by a concentrated radial load. Two cases are considered. In the first case the loaded end cross section is closed by a rigid plate and in the second case the radial load is applied immediately to it. The paper gives solutions for radial displacements, slips and stresses. The presented examples can be used as benchmark for the other types of solutions as given in this study.

scholarly journals CRITICAL EXPERIMENT OF THORIUM LOADED THERMAL CORES AT KUCA (1) A NEW CRITICAL EXPERIMENT OF THORIUM LOADED CORE WITH HARDER NEUTRON SPECTRUM IN KUCA

2021 ◽  
Vol 247 ◽  
pp. 09013
Author(s):  
Tadafumi Sano ◽  
Jun-ichi Hori ◽  
Jeaong Lee ◽  
Yoshiyuki Takahashi ◽  
Kazuki Takahashi ◽  
...  
Keyword(s):  
Cross Section ◽  
Neutron Spectrum ◽  
Cross Sections ◽  
Capture Cross Section ◽  
The Other ◽  
Capture Cross ◽  
Delayed Neutron ◽  
Integral Evaluation ◽  
Critical Experiment ◽  
The Difference

In order to perform integral evaluation of 232Th capture cross section, a series of critical experiments for thorium-loaded and solid-moderated cores in KUCA had been carried out. In these experimental cores, H/235U nuclide ratio ranged about from 150 to 315, and 232Th/235U nuclide ratio ranged about from 13 to 19. In this study, a new critical experiment with Th loaded core in KUCA, which had about 70 of the H/235U ratio and 12.7 of 232Th/235U ratio, was carried out. As results, the excess reactivity was 0.086 ± 0.003 (% dk/k) and the keff was 1.0009 ± 0.0003, where the effective delayed neutron fraction was 7.656E-3. The keff was also calculated by MVP3.0 with different nuclear libraries. The respective calculations with JENDL-4.0, JENDL-3.3 and ENDF/B-VII.0 lead to 1.0056 ± 0.0086 (%), 1.0048 ± 0.0085 (%) and 1.0056 ± 0.0086 (%).On the other hand, the further MVP3.0 calculations, where only the 232Th cross sections were taken from JENDL-4.0, JENDL-3.3 or ENDF/B-VII.0 but all other nuclides were done from JENDL-4.0, were carried out to examine an impact of the difference of 232Th cross section among these nuclear libraries to the keff. The keff calculated with respective 232Th cross sections from JENDL-3.3 and ENDF/B-VII.0 was 1.0038 ± 0.0086 (%) and 1.0040 ± 0.0086 (%).

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