Document Detail

The chromodomain-containing NH(2)-terminus of Chromator interacts with histone H1 and is required for correct targeting to chromatin.
MedLine Citation:
PMID:  22203189     Owner:  NLM     Status:  MEDLINE    
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.
Changfu Yao; Yun Ding; Weili Cai; Chao Wang; Jack Girton; Kristen M Johansen; Jørgen Johansen
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2011-12-28
Journal Detail:
Title:  Chromosoma     Volume:  121     ISSN:  1432-0886     ISO Abbreviation:  Chromosoma     Publication Date:  2012 Apr 
Date Detail:
Created Date:  2012-03-22     Completed Date:  2012-07-13     Revised Date:  2014-09-16    
Medline Journal Info:
Nlm Unique ID:  2985138R     Medline TA:  Chromosoma     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  209-20     Citation Subset:  IM    
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MeSH Terms
Chromatin / chemistry*,  metabolism*
Drosophila Proteins / metabolism*
Drosophila melanogaster / genetics,  metabolism*
Electrophoresis, Polyacrylamide Gel
Genetic Vectors / genetics
Histones / metabolism*
Interphase / physiology*
Models, Molecular*
Nuclear Matrix-Associated Proteins / metabolism*
Protein Structure, Tertiary
Grant Support
Reg. No./Substance:
0/Chromatin; 0/Drosophila Proteins; 0/Histones; 0/Nuclear Matrix-Associated Proteins; 0/chromator protein, Drosophila

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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