The chromodomain protein, Chromator, can be divided into two main domains, a 
NH(2)-terminal domain (NTD) containing the chromodomain (ChD) and a 
COOH-terminal domain (CTD) containing a nuclear localization signal. During 
interphase Chromator is localized to chromosomes; however, during cell division 
Chromator redistributes to form a macro molecular spindle matrix complex 
together with other nuclear proteins that contribute to microtubule spindle 
dynamics and proper chromosome segregation during mitosis. It has previously 
been demonstrated that the CTD is sufficient for targeting Chromator to the 
spindle matrix. In this study, we show that the NTD domain of Chromator is 
required for proper localization to chromatin during interphase and that 
chromosome morphology defects observed in Chromator hypomorphic mutant 
backgrounds can be largely rescued by expression of this domain. Furthermore, we 
show that the ChD domain can interact with histone H1 and that this interaction 
is necessary for correct chromatin targeting. Nonetheless, that localization to 
chromatin still occurs in the absence of the ChD indicates that Chromator 
possesses a second mechanism for chromatin association and we provide evidence 
that this association is mediated by other sequences residing in the NTD. Taken 
together these findings suggest that Chromator's chromatin functions are largely 
governed by the NH(2)-terminal domain whereas functions related to mitosis are 
mediated mainly by COOH-terminal sequences.