![[Feedback]](/icons/banner/feedbackACT.gif){kind=icon}
![[For Subscribers]](/icons/banner/subscriberACT.gif){kind=icon}
![[Archive]](/icons/banner/archiveACT.gif){kind=icon}
![[Search]](/icons/banner/searchACT.gif){kind=icon}
![[Contents]](/icons/banner/tocACT.gif){kind=icon}
|
|
|
|
|
||
KA Kandl, JD Forney and DJ Asai
Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA.
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.
This article has been cited by other articles:
|
|
 |
|
  M. Levin THE EMBRYONIC ORIGINS OF LEFT-RIGHT ASYMMETRY Critical Reviews in Oral Biology & Medicine, July 1, 2004; 15(4): 197 - 206. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. H. Myster, J. A. Knott, K. M. Wysocki, E. O'Toole, and M. E. Porter Domains in the 1{alpha} Dynein Heavy Chain Required for Inner Arm Assembly and Flagellar Motility in Chlamydomonas J. Cell Biol., August 23, 1999; 146(4): 801 - 818. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. E. Porter, R. Bower, J. A. Knott, P. Byrd, and W. Dentler Cytoplasmic Dynein Heavy Chain 1b Is Required for Flagellar Assembly in Chlamydomonas Mol. Biol. Cell, March 1, 1999; 10(3): 693 - 712. [Abstract] [Full Text]
|
|
|
|
 |
|
 D. Supp, M Brueckner, M. Kuehn, D. Witte, L. Lowe, J McGrath, J Corrales, and S. Potter Targeted deletion of the ATP binding domain of left-right dynein confirms its role in specifying development of left-right asymmetries Development, January 12, 1999; 126(23): 5495 - 5504. [Abstract] [PDF]
|
|
|
|
 |
|
 P. Criswell, L. Ostrowski, and D. Asai A novel cytoplasmic dynein heavy chain: expression of DHC1b in mammalian ciliated epithelial cells J. Cell Sci., January 7, 1996; 109(7): 1891 - 1898. [Abstract] [PDF]
|
|
|
|
 |
|
 J. L. Carson, W. Reed, T. Lucier, L. Brighton, T. M. Gambling, C.-H. Huang, and A. M. Collier Pre- and Postnatal Lung Development, Maturation, and Plasticity: Axonemal dynein expression in human fetal tracheal epithelium Am J Physiol Lung Cell Mol Physiol, March 1, 2002; 282(3): L421 - L430. [Abstract] [Full Text] [PDF]
|
|
