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Vol. 11, Issue 7, 2297-2313, July 2000
Dynein Heavy Chain
and
*Department of Genetics, Cell Biology, and Development, University
of Minnesota Medical School, Minneapolis, Minnesota 55455; and
To identify domains in the dynein heavy chain (Dhc) required for
the assembly of an inner arm dynein, we characterized a new motility
mutant (ida2-6) obtained by insertional mutagenesis. ida2-6 axonemes lack the polypeptides associated with
the I1 inner arm complex. Recovery of genomic DNA flanking the mutation
indicates that the defects are caused by plasmid insertion into the
Dhc10 transcription unit, which encodes the 1Department of Molecular, Cellular, and Developmental
Biology, University of Colorado at Boulder, Boulder, Colorado 80309
Dhc of
the I1 complex. Transformation with Dhc10 constructs
encoding <20% of the Dhc can partially rescue the motility defects by
reassembly of an I1 complex containing an N-terminal 1 Dhc fragment
and a full-length 1
Dhc. Electron microscopic analysis reveals the
location of the missing 1 Dhc motor domain within the axoneme
structure. These observations, together with recent studies on the 1
Dhc, identify a Dhc domain required for complex assembly and further demonstrate that the intermediate and light chains are associated with
the stem regions of the Dhcs in a distinct structural location. The
positioning of these subunits within the I1 structure has significant
implications for the pathways that target the assembly of the I1
complex into the axoneme and modify the activity of the I1 dynein
during flagellar motility.
Present address: Department of Biology,
Coker Hall, CB#3280, University of North Carolina at Chapel Hill,
Chapel Hill, NC 27599-3280.
§
Corresponding author. E-mail address:
mary-p{at}biosci.cbs.umn.edu.
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