scholarly journals Novel 44-Kilodalton Subunit of Axonemal Dynein Conserved from Chlamydomonas to Mammals

2007 ◽  
Vol 7 (1) ◽  
pp. 154-161 ◽  
Author(s):  
Ryosuke Yamamoto ◽  
Haru-aki Yanagisawa ◽  
Toshiki Yagi ◽  
Ritsu Kamiya
Keyword(s):  
Heavy Chain ◽  
Docking Site ◽  
Mouse Homologue ◽  
Axonemal Dynein ◽  
Motile Cilia ◽  
Cilia And Flagella ◽  
Subunit Organization

ABSTRACT Cilia and flagella have multiple dyneins in their inner and outer arms. Chlamydomonas inner-arm dynein contains at least seven major subspecies (dynein a to dynein g), of which all but dynein f (also called dynein I1) are the single-headed type that are composed of a single heavy chain, actin, and either centrin or a 28-kDa protein (p28). Dynein d was found to associate with two additional proteins of 38 kDa (p38) and 44 kDa (p44). Following the characterization of the p38 protein (R. Yamamoto, H. A. Yanagisawa, T. Yagi, and R. Kamiya, FEBS Lett. 580:6357-6360, 2006), we have identified p44 as a novel component of dynein d by using an immunoprecipitation approach. p44 is present along the length of the axonemes and is diminished, but not absent, in the ida4 and ida5 mutants, both lacking this dynein. In the ida5 axoneme, p44 and p38 appear to form a complex, suggesting that they constitute the docking site of dynein d on the outer doublet. p44 has potential homologues in other ciliated organisms. For example, the mouse homologue of p44, NYD-SP14, was found to be strongly expressed in tissues with motile cilia and flagella. These results suggest that inner-arm dynein d and its subunit organization are widely conserved.

scholarly journals Characterization of an Axonemal Dynein Heavy Chain Expressed Early in Airway Epithelial Ciliogenesis

2000 ◽  
Vol 23 (6) ◽  
pp. 734-741 ◽  
Author(s):  
William Reed ◽  
Johnny L. Carson ◽  
Billie M. Moats-Staats ◽  
Thomas Lucier ◽  
Ping-chuan Hu ◽  
...  
Keyword(s):  
Heavy Chain ◽  
Airway Epithelial ◽  
Dynein Heavy Chain ◽  
Axonemal Dynein

scholarly journals Cytoplasmic factories for axonemal dynein assembly

2021 ◽  
Vol 134 (15) ◽  
Author(s):  
Stephen M. King
Keyword(s):  
Heavy Chain ◽  
Meta Analysis ◽  
Direct Consequence ◽  
Assembly Process ◽  
Dynein Heavy Chain ◽  
Axonemal Dynein ◽  
Cilia And Flagella ◽  
Chain Synthesis ◽  
Set Up

ABSTRACT Axonemal dyneins power the beating of motile cilia and flagella. These massive multimeric motor complexes are assembled in the cytoplasm, and subsequently trafficked to cilia and incorporated into the axonemal superstructure. Numerous cytoplasmic factors are required for the dynein assembly process, and, in mammals, defects lead to primary ciliary dyskinesia, which results in infertility, bronchial problems and failure to set up the left-right body axis correctly. Liquid–liquid phase separation (LLPS) has been proposed to underlie the formation of numerous membrane-less intracellular assemblies or condensates. In multiciliated cells, cytoplasmic assembly of axonemal dyneins also occurs in condensates that exhibit liquid-like properties, including fusion, fission and rapid exchange of components both within condensates and with bulk cytoplasm. However, a recent extensive meta-analysis suggests that the general methods used to define LLPS systems in vivo may not readily distinguish LLPS from other mechanisms. Here, I consider the time and length scales of axonemal dynein heavy chain synthesis, and the possibility that during translation of dynein heavy chain mRNAs, polysomes are crosslinked via partially assembled proteins. I propose that axonemal dynein factory formation in the cytoplasm may be a direct consequence of the sheer scale and complexity of the assembly process itself.

scholarly journals Dynein-2 Affects the Regulation of Ciliary Length but Is Not Required for Ciliogenesis in Tetrahymena thermophila

2009 ◽  
Vol 20 (2) ◽  
pp. 708-720 ◽  
Author(s):  
Vidyalakshmi Rajagopalan ◽  
Aswati Subramanian ◽  
David E. Wilkes ◽  
David G. Pennock ◽  
David J. Asai
Keyword(s):  
Electron Microscopy ◽  
Cell Lines ◽  
Heavy Chain ◽  
Tetrahymena Thermophila ◽  
Intraflagellar Transport ◽  
Cytoplasmic Dynein ◽  
Wild Type ◽  
Mild Phenotype ◽  
Motile Cilia ◽  
Cilia And Flagella

Eukaryotic cilia and flagella are assembled and maintained by the bidirectional intraflagellar transport (IFT). Studies in alga, nematode, and mouse have shown that the heavy chain (Dyh2) and the light intermediate chain (D2LIC) of the cytoplasmic dynein-2 complex are essential for retrograde intraflagellar transport. In these organisms, disruption of either dynein-2 component results in short cilia/flagella with bulbous tips in which excess IFT particles have accumulated. In Tetrahymena, the expression of the DYH2 and D2LIC genes increases during reciliation, consistent with their roles in IFT. However, the targeted elimination of either DYH2 or D2LIC gene resulted in only a mild phenotype. Both knockout cell lines assembled motile cilia, but the cilia were of more variable lengths and less numerous than wild-type controls. Electron microscopy revealed normally shaped cilia with no swelling and no obvious accumulations of material in the distal ciliary tip. These results demonstrate that dynein-2 contributes to the regulation of ciliary length but is not required for ciliogenesis in Tetrahymena.

scholarly journals Tubulin glycylation controls axonemal dynein activity, flagellar beat, and male fertility

Science ◽  
2021 ◽  
Vol 371 (6525) ◽  
pp. eabd4914
Author(s):  
Sudarshan Gadadhar ◽  
Gonzalo Alvarez Viar ◽  
Jan Niklas Hansen ◽  
An Gong ◽  
Aleksandr Kostarev ◽  
...  
Keyword(s):  
Posttranslational Modifications ◽  
Male Fertility ◽  
Electron Tomography ◽  
Structural Basis ◽  
Cellular Functions ◽  
Flagellar Beat ◽  
Cryo Electron Tomography ◽  
Axonemal Dynein ◽  
Dynein Arms ◽  
Cilia And Flagella

Posttranslational modifications of the microtubule cytoskeleton have emerged as key regulators of cellular functions, and their perturbations have been linked to a growing number of human pathologies. Tubulin glycylation modifies microtubules specifically in cilia and flagella, but its functional and mechanistic roles remain unclear. In this study, we generated a mouse model entirely lacking tubulin glycylation. Male mice were subfertile owing to aberrant beat patterns of their sperm flagella, which impeded the straight swimming of sperm cells. Using cryo–electron tomography, we showed that lack of glycylation caused abnormal conformations of the dynein arms within sperm axonemes, providing the structural basis for the observed dysfunction. Our findings reveal the importance of microtubule glycylation for controlled flagellar beating, directional sperm swimming, and male fertility.

scholarly journals Gamma heavy chain disease: clinical aspects and characterization of a deleted, noncovalently linked gamma1 heavy chain dimer (BAZ)

Blood ◽  
1977 ◽  
Vol 49 (4) ◽  
pp. 495-505 ◽  
Author(s):  
GB Faguet ◽  
BP Barton ◽  
LL Smith ◽  
FA Garver
Keyword(s):  
Heavy Chain ◽  
Plasma Cells ◽  
Clinical Feature ◽  
Clinical Aspects ◽  
Submaxillary Glands ◽  
Underlying Malignancy ◽  
V Region ◽  
Allotypic Marker ◽  
Heavy Chain Disease

Abstract This report describes the clinical and immunoglobulin features of a patient with gamma heavy chain disease (HCD), who presented with a clinical picture suggestive of an underlying malignancy rather than the usual picture of lymphoma or granulomatous disease. A unique clinical feature was the nearly total replacement of the submaxillary glands by plasma cells. The patient's serum and urine contained a paraprotein, gammaHCD protein BAZ, which belongs to the gamma1 subclass and forms noncovalently linked dimers with a molecular weight of approximately 60,000 daltons. This mutant protein exhibited a deletion which encompassed most of the variable (V) region, the first constant domain (CH 1), and the hinge region. In addition, preliminary structural analyses demonstrated the replacement of alanine by glycine in position 431 of the carboxyterminal octadecapeptide. This substitution may possibly represent another allotypic marker on IgG1 proteins.

scholarly journals Characterization of a strong positive cis-acting element of the human beta-myosin heavy chain gene in fetal rat heart cells.

1992 ◽  
Vol 267 (14) ◽  
pp. 9917-9924 ◽  
Author(s):  
I.L. Flink ◽  
J.G. Edwards ◽  
J.J. Bahl ◽  
C.C. Liew ◽  
M Sole ◽  
...  
Keyword(s):  
Heavy Chain ◽  
Rat Heart ◽  
Chain Gene ◽  
Heart Cells ◽  
Heavy Chain Gene ◽  
Myosin Heavy Chain Gene ◽  
Cis Acting ◽  
Fetal Rat ◽  
Rat Heart Cells

scholarly journals Inversions produced during V(D)J rearrangement at IgH, the immunoglobulin heavy-chain locus.

1995 ◽  
Vol 15 (2) ◽  
pp. 671-681 ◽  
Author(s):  
A E Sollbach ◽  
G E Wu
Keyword(s):  
Heavy Chain ◽  
Adult Mouse ◽  
Fetal Liver ◽  
Immunoglobulin Heavy Chain ◽  
Antigen Receptors ◽  
Adult Mice ◽  
Chain Locus ◽  
Heavy Chain Locus ◽  
Fetal Liver Cells

Diversity in immunoglobulin antigen receptors is generated in part by V(D)J recombination. In this process, different combinations of gene elements are joined in various configurations. Products of V(D)J recombination are coding joints, signal joints, and hybrid junctions, which are generated by deletion or inversion. To determine their role in the generation of diversity, we have examined two sorts of recombination products, coding joints and hybrid junctions, that have formed by inversion at the mouse immunoglobulin heavy-chain locus. We developed a PCR assay for quantification and characterization of inverted rearrangements of DH and JH gene elements. In primary cells from adult mice, inverted DJH rearrangements are detectable but they are rare. There were approximately 1,100 to 2,200 inverted DJH coding joints and inverted DJH hybrid junctions in the marrow of one adult mouse femur. On day 16 of gestation, inverted DJH rearrangements are more abundant. There are approximately 20,000 inverted DJH coding joints and inverted DJH hybrid junctions per day 16 fetal liver. In fetal liver cells, the number of inverted DJH rearrangements remains relatively constant from day 14 to day 16 of gestation. Inverted DJH rearrangements to JH4, the most 3' JH element, are more frequently detected than inverted DJH rearrangements to other JH elements. We compare the frequencies of inverted DJH rearrangements to previously determined frequencies of uninverted DJH rearrangements (DJH rearrangements formed by deletion). We suggest that inverted DJH rearrangements are influenced by V(D)J recombination mechanistic constraints and cellular selection.

scholarly journals Characterization of a Temperature-Sensitive Vertebrate Clathrin Heavy Chain Mutant as a Tool to Study Clathrin-Dependent Events In Vivo

PLoS ONE ◽  
2010 ◽  
Vol 5 (8) ◽  
pp. e12017 ◽  
Author(s):  
Petra Neumann-Staubitz ◽  
Stephanie L. Hall ◽  
Joseph Kuo ◽  
Antony P. Jackson
Keyword(s):  
Heavy Chain ◽  
Temperature Sensitive ◽  
Clathrin Heavy Chain
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