Literature DB >> 8589455

The dynein genes of Paramecium tetraurelia: the structure and expression of the ciliary beta and cytoplasmic heavy chains.

K A Kandl1, J D Forney, D J Asai.   

Abstract

The genes encoding two Paramecium dynein heavy chains, DHC-6 and DHC-8, have been cloned and sequenced. Sequence-specific antibodies demonstrate that DHC-6 encodes ciliary outer arm beta-chain and DHC-8 encodes a cytoplasmic dynein heavy chain. Therefore, this study is the first opportunity to compare the primary structures and expression of two heavy chains representing the two functional classes of dynein expressed in the same cell. Deciliation of paramecia results in the accumulation of mRNA from DHC-6, but not DHC-8. Nuclear run-on transcription experiments demonstrate that this increase in the steady state concentration of DHC-6 mRNA is a consequence of a rapid induction of transcription in response to deciliation. This is the first demonstration that dynein, like other axonemal components, is transcriptionally regulated during reciliation. Analyses of the sequences of the two Paramecium dyneins and the dynein heavy chains from other organisms indicate that the heavy chain can be divided into three regions: 1) the sequence of the central catalytic domain is conserved among all dyneins; 2) the tail domain sequence, consisting of the N-terminal 1200 residues, differentiates between axonemal and cytoplasmic dyneins; and 3) the N-terminal 200 residues are the most divergent and appear to classify the isoforms. The organization of the heavy chain predicts that the variable tail domain may be sufficient to target the dynein to the appropriate place in the cell.

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Year:  1995        PMID: 8589455      PMCID: PMC301310          DOI: 10.1091/mbc.6.11.1549

Source DB:  PubMed          Journal:  Mol Biol Cell        ISSN: 1059-1524            Impact factor:   4.138


  65 in total

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Authors:  J Larsen; K Barkalow; T Hamasaki; P Satir
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9.  Cytoplasmic dynein-dependent vesicular transport from early to late endosomes.

Authors:  F Aniento; N Emans; G Griffiths; J Gruenberg
Journal:  J Cell Biol       Date:  1993-12       Impact factor: 10.539

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Authors:  J P Lees-Miller; D M Helfman; T A Schroer
Journal:  Nature       Date:  1992-09-17       Impact factor: 49.962

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  5 in total

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Authors:  M E Porter; R Bower; J A Knott; P Byrd; W Dentler
Journal:  Mol Biol Cell       Date:  1999-03       Impact factor: 4.138

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3.  Targeted deletion of the ATP binding domain of left-right dynein confirms its role in specifying development of left-right asymmetries.

Authors:  D M Supp; M Brueckner; M R Kuehn; D P Witte; L A Lowe; J McGrath; J Corrales; S S Potter
Journal:  Development       Date:  1999-12       Impact factor: 6.868

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Authors:  E A Vaisberg; P M Grissom; J R McIntosh
Journal:  J Cell Biol       Date:  1996-05       Impact factor: 10.539

5.  Domains in the 1alpha dynein heavy chain required for inner arm assembly and flagellar motility in Chlamydomonas.

Authors:  S H Myster; J A Knott; K M Wysocki; E O'Toole; M E Porter
Journal:  J Cell Biol       Date:  1999-08-23       Impact factor: 10.539

  5 in total

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