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A split motor domain in a cytoplasmic dynein
1Institut für Genetik und Mikrobiologie, LMU, Maria-Ward-Strasse 1a, D-80638 München, Germany.
The EMBO Journal
|September 22, 2001
Summary
In Ustilago maydis, two genes, dyn1 and dyn2, encode the dynein heavy chain. These proteins form a complex essential for cell survival, nuclear migration, and morphogenesis.
Area of Science:
- Cell Biology
- Molecular Biology
- Mycology
Background:
- Dynein is a motor protein crucial for intracellular transport and cellular functions.
- The heavy chain of dynein contains the motor domain, ATP-cleavage, and microtubule-binding sites.
Purpose of the Study:
- To investigate the genes encoding the dynein heavy chain in Ustilago maydis.
- To determine the interaction and functional relationship between the encoded dynein heavy chain polypeptides.
Main Methods:
- Gene identification and characterization (dyn1 and dyn2).
- Co-immunoprecipitation and co-localization studies.
- Analysis of Dyn1-Dyn2 fusion proteins and conditional mutants.
Main Results:
- Ustilago maydis possesses two dynein heavy chain genes, dyn1 and dyn2, on separate chromosomes.
- Dyn1 and Dyn2 proteins interact to form a complex essential for cell survival.
- The Dyn1-Dyn2 complex is involved in nuclear migration, cell morphogenesis, and microtubule organization.
Conclusions:
- The dynein heavy chain in Ustilago maydis is encoded by two distinct genes, dyn1 and dyn2.
- These polypeptides form a functional complex with essential roles in multiple cellular processes.
- Dyn1 contributes to microtubule binding, while Dyn2 provides the ATPase region, highlighting functional specialization within the complex.
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