The chromodomain-containing NH sub(2)-terminus of Chromator interacts with histone H1 and is required for correct targeting to chromatin

The chromodomain protein, Chromator, can be divided into two main domains, a NH sub(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 divi...

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Veröffentlicht in:Chromosoma 2012-04, Vol.121 (2), p.209-220
Hauptverfasser: Yao, Changfu, Ding, Yun, Cai, Weili, Wang, Chao, Girton, Jack, Johansen, Kristen M, Johansen, Joergen
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container_end_page 220
container_issue 2
container_start_page 209
container_title Chromosoma
container_volume 121
creator Yao, Changfu
Ding, Yun
Cai, Weili
Wang, Chao
Girton, Jack
Johansen, Kristen M
Johansen, Joergen
description The chromodomain protein, Chromator, can be divided into two main domains, a NH sub(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 sub(2)-terminal domain whereas functions related to mitosis are mediated mainly by COOH-terminal sequences.
doi_str_mv 10.1007/s00412-011-0355-4
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title The chromodomain-containing NH sub(2)-terminus of Chromator interacts with histone H1 and is required for correct targeting to chromatin
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