Functional and molecular diversity of dynein heavy chains

1996 ◽  
Vol 7 (3) ◽  
pp. 311-320 ◽  
Author(s):  
David J. Asai
Keyword(s):  
Molecular Diversity ◽  
Heavy Chains ◽  
Dynein Heavy Chains

scholarly journals Chymotryptic digestion of Tetrahymena ciliary dynein. II. Pathway of the degradation of 22S dynein heavy chains.

1987 ◽  
Vol 105 (2) ◽  
pp. 897-901 ◽  
Author(s):  
Y Y Toyoshima
Keyword(s):  
Atpase Activity ◽  
Gel Electrophoresis ◽  
Peptide Mapping ◽  
Preceding Paper ◽  
Degradation Pathway ◽  
Heavy Chains ◽  
Cell Biol ◽  
Dynein Heavy Chains

As shown in the preceding paper (Toyoshima, Y. Y., 1987, J. Cell Biol., 105:887-895) three-headed Tetrahymena 22S dynein consists of three heavy chains (HCs) and is decomposed into two-headed (H) and one-headed (L) fragments by chymotryptic digestion. To accurately determine the presence of multiple ATPases and ultimately the location of various domains, it is necessary to determine the identity of each HC fragment relative to the original HCs in 22S dynein. The degradation pathway of each HC was determined by peptide mapping and immunoblotting. The three HCs (A alpha, A beta, and A gamma) were immunologically different; although SDS-urea gel electrophoresis showed that A gamma HC was apparently resistant to the digestion, actually three distinct HCs contributed to the same band alternately. H fragment was derived from A beta and A gamma HCs, whereas L fragment originated from A alpha HC. Since both fragments were associated with ATPase activity, these results directly demonstrate the presence of multiple ATPase sites in Tetrahymena 22S dynein.

scholarly journals The intraflagellar transport dynein complex of trypanosomes is made of a heterodimer of dynein heavy chains and of light and intermediate chains of distinct functions

2014 ◽  
Vol 25 (17) ◽  
pp. 2620-2633 ◽  
Author(s):  
Thierry Blisnick ◽  
Johanna Buisson ◽  
Sabrina Absalon ◽  
Alexandra Marie ◽  
Nadège Cayet ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Intraflagellar Transport ◽  
Retrograde Transport ◽  
High Concentration ◽  
Anterograde Transport ◽  
Heavy Chains ◽  
Cilia And Flagella ◽  
The Stability ◽  
Intermediate Chains ◽  
Dynein Heavy Chains

Cilia and flagella are assembled by intraflagellar transport (IFT) of protein complexes that bring tubulin and other precursors to the incorporation site at their distal tip. Anterograde transport is driven by kinesin, whereas retrograde transport is ensured by a specific dynein. In the protist Trypanosoma brucei, two distinct genes encode fairly different dynein heavy chains (DHCs; ∼40% identity) termed DHC2.1 and DHC2.2, which form a heterodimer and are both essential for retrograde IFT. The stability of each heavy chain relies on the presence of a dynein light intermediate chain (DLI1; also known as XBX-1/D1bLIC). The presence of both heavy chains and of DLI1 at the base of the flagellum depends on the intermediate dynein chain DIC5 (FAP133/WDR34). In the IFT140RNAi mutant, an IFT-A protein essential for retrograde transport, the IFT dynein components are found at high concentration at the flagellar base but fail to penetrate the flagellar compartment. We propose a model by which the IFT dynein particle is assembled in the cytoplasm, reaches the base of the flagellum, and associates with the IFT machinery in a manner dependent on the IFT-A complex.

High molecular weight polypeptides related to dynein heavy chains in Nicotiana tabacum pollen tubes

1995 ◽  
Vol 108 (3) ◽  
pp. 1117-1125
Author(s):  
A. Moscatelli ◽  
C. Del Casino ◽  
L. Lozzi ◽  
G. Cai ◽  
M. Scali ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Nicotiana Tabacum ◽  
Pollen Tube ◽  
High Molecular Weight ◽  
Pollen Tubes ◽  
Biochemical Properties ◽  
Bovine Brain ◽  
Atp Binding ◽  
Heavy Chains ◽  
Dynein Heavy Chains

Nicotiana tabacum pollen tubes contain two high molecular weight polypeptides (about 400 kDa), which are specifically expressed during pollen germination and pollen tube growth in BK medium. The high molecular weight doublet resembles the dynein heavy chains in some biochemical properties. Sedimentation profiles of pollen tube extracts show that the high molecular weight bands have sedimentation coefficients of 22 S and 12 S, respectively. ATPase assay of sedimentation fractions shows an activity ten times higher when stimulated by the presence of bovine brain microtubules in fractions containing the 22 S high molecular weight polypeptide. Both these high molecular weight polypeptides can bind microtubules in an ATP-dependent fashion. A mouse antiserum to a synthetic peptide reproducing the sequence of the most conserved ATP-binding site among dynein heavy chains recognized the two high molecular weight polypeptides. Therefore these polypeptides have sequences immunologically related to the ATP binding sites of dynein heavy chains.

scholarly journals Asymmetry of inner dynein arms and inter-doublet links in Chlamydomonas flagella

2009 ◽  
Vol 186 (3) ◽  
pp. 437-446 ◽  
Author(s):  
Khanh Huy Bui ◽  
Hitoshi Sakakibara ◽  
Tandis Movassagh ◽  
Kazuhiro Oiwa ◽  
Takashi Ishikawa
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Heavy Chain ◽  
Single Particle ◽  
Heavy Chains ◽  
Molecular Arrangement ◽  
Dynein Arms ◽  
Electron Cryotomography ◽  
Microtubule Doublet ◽  
Asymmetrical Bending ◽  
Dynein Heavy Chains

Although the widely shared “9 + 2” structure of axonemes is thought to be highly symmetrical, axonemes show asymmetrical bending during planar and conical motion. In this study, using electron cryotomography and single particle averaging, we demonstrate an asymmetrical molecular arrangement of proteins binding to the nine microtubule doublets in Chlamydomonas reinhardtii flagella. The eight inner arm dynein heavy chains regulate and determine flagellar waveform. Among these, one heavy chain (dynein c) is missing on one microtubule doublet (this doublet also lacks the outer dynein arm), and another dynein heavy chain (dynein b or g) is missing on the adjacent doublet. Some dynein heavy chains either show an abnormal conformation or were replaced by other proteins, possibly minor dyneins. In addition to nexin, there are two additional linkages between specific pairs of doublets. Interestingly, all these exceptional arrangements take place on doublets on opposite sides of the axoneme, suggesting that the transverse functional asymmetry of the axoneme causes an in-plane bending motion.

Characterisation of boar sperm dynein heavy chains by UV vanadate dependent photocleavage

1994 ◽  
Vol 82 (2-3) ◽  
pp. 203-210 ◽  
Author(s):  
Jean-Luc Gatti ◽  
Jean-Claude Nicolle ◽  
Jean-Louis Dacheux
Keyword(s):  
Heavy Chains ◽  
Boar Sperm ◽  
Dynein Heavy Chains

scholarly journals ida4-1, ida4-2, and ida4-3 are intron splicing mutations affecting the locus encoding p28, a light chain of Chlamydomonas axonemal inner dynein arms.

1995 ◽  
Vol 6 (6) ◽  
pp. 713-723 ◽  
Author(s):  
M LeDizet ◽  
G Piperno
Keyword(s):  
Nucleotide Sequence ◽  
Light Chain ◽  
Polymerase Chain Reaction Amplification ◽  
Intron Splicing ◽  
Gene Encoding ◽  
Heavy Chains ◽  
Single Nucleotide Change ◽  
Splicing Mutations ◽  
Dynein Arms ◽  
Dynein Heavy Chains

We recently determined the nucleotide sequence of the gene encoding p28, a light chain of inner dynein arms of Chlamydomonas axonemes. Here, we show that p28 is the protein encoded by the IDA4 locus. p28, and the dynein heavy chains normally associated with it, are completely absent from the flagella and cell bodies of three allelic strains of ida4, named ida4-1, ida4-2, and ida4-3. We determined the nucleotide sequence of the three alleles of the p28 gene and found in each case a single nucleotide change, affecting the splice sites of the first, second, and fourth introns, respectively. Reverse transcriptase-polymerase chain reaction amplification of RNAs prepared from ida4 cells confirmed that these mutations prevent the correct splicing of the affected introns, thereby blocking the synthesis of full-length p28. These are the first intron splicing mutations described in Chlamydomonas and the first inner dynein arm mutations characterized at the molecular level. The absence in ida4 axonemes of the dynein heavy chains normally found in association with p28 suggests that p28 is necessary for stable assembly of a subset of inner dynein arms or for the binding of these arms to the microtubule doublets.

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