Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1931475 | Biochemical and Biophysical Research Communications | 2010 | 5 Pages |
The Dam1 complex is an important part of the yeast kinetochore. It mediates attachment of the chromosome to the mitotic spindle and is involved in chromatid separation initiated at anaphase. It is comprised of 10 individual subunits and has been observed to oligomerize in various ways as it interacts with microtubules, including forming a ring. This work explores the biochemical and biophysical properties of Dad1, one of the Dam1 complex subunits from the human fungal pathogen Candida albicans. Unlike its Saccharomyces cerevisiae counterpart, C. albicans Dad1 can be expressed as a soluble protein in Escherichia coli. Analysis of this protein’s hydrodynamic properties, thermostability and primary sequence have been conducted. As a result, we conclude that isolated Dad1 is an intrinsically disordered protein.
Research highlights► The Dad1 subunit of the C. albicans Dam1 complex was isolated. ► Dad1 was shown to be thermostable. ► Hydrodynamic analysis of Dad1 was conducted under native and denaturing conditions. ► Our results suggest that Dad1 is an intrinsically disordered protein.