2010
DOI: 10.1016/j.bbrc.2010.08.050
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The Dad1 subunit of the yeast kinetochore Dam1 complex is an intrinsically disordered protein

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Cited by 4 publications
(2 citation statements)
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“…First, we identified putative C. albicans homologs of Dam1 complex members (Figure 1A and Table S1). The C. albicans Dad1 homolog is an intrinsically disordered protein with a structure similar to that of S. cerevisiae Dad1 [11]. By chromatin immunoprecipitation (ChIP), Dad1-GFP and Dam1-GFP bind centromere DNA regions that co-localize with regions bound by CENP-A (Figure 1B).…”
Section: Resultsmentioning
confidence: 99%
“…First, we identified putative C. albicans homologs of Dam1 complex members (Figure 1A and Table S1). The C. albicans Dad1 homolog is an intrinsically disordered protein with a structure similar to that of S. cerevisiae Dad1 [11]. By chromatin immunoprecipitation (ChIP), Dad1-GFP and Dam1-GFP bind centromere DNA regions that co-localize with regions bound by CENP-A (Figure 1B).…”
Section: Resultsmentioning
confidence: 99%
“…We have been examining the individual subunits of the Dam1 complex from Candida albicans, as some of these proteins are capable of being expressed in bacteria. For example, the C. albicans Dad1p has been shown to behave as an intrinsically disordered protein when isolated (J. T. Waldo, Greagor, Iqbal, Gittens, & Grant, 2010). Based on these studies, a working model is that Dad1p undergoes a structural transition upon binding to the other components of the complex.…”
Section: Introductionmentioning
confidence: 99%