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Volumn 10, Issue 2, 2000, Pages 204-210

The HP1 protein family: Getting a grip on chromatin

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN;

EID: 0034026194     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(00)00058-7     Document Type: Review
Times cited : (406)

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    • Phosphorylation of heterochromatin protein 1 by casein kinase II is required for efficient heterochromatin binding in Drosophila
    • This group previously showed that HP1 is multiply phosphorylated and that hyperphosphorylation is correlated with heterochromatin assembly. In this paper, they report that three phosphorylation sites are targets for casein kinase II (CKII). Alanine substitution mutations that block CKII phosphorylation interfere with efficient heterochromatin targeting by HP1.
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    • This paper reports a detailed analysis of the nuclear distribution of the three known human HP1 family members during the cell cycle. Two of the three are heterochromatin-associated, while the third is dispersed at numerous euchromatic sites. The authors also show that two of the three are phosphorylated, with more extensive phosphorylation associated with M phase in the cell cycle.
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    • A previous study demonstrated that arrays of P-elements containing a white transgene resulted in variegated silencing of white. Silencing appeared to be a result of the assembly of ectopic heterochromatin at the array locus. This paper shows that the silenced arrays recruit HP1. Interestingly, a single copy white transgene, which shows no variegation, still binds HP1, suggesting that HP1-dependent silencing might require threshold quantities of HP1.
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    • The authors exploit previously established transgenic mouse lines in which a human D2 locus control region mutation construct was found to variegate when inserted in heterochromatin. This paper shows that the variegation is enhanced by overexpression of mouse M31. This is the first demonstration of dosage-dependent silencing by an HP1 family protein in a metazoan other than Drosophila.
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    • The HP1 chromo shadow domain binds a consensus peptide pentamer
    • By probing a random phage display library with a Drosophila HP1 chromo shadow domain, the authors identify a consensus peptide motif sufficient for chromo shadow domain binding. Sequences highly related to this consensus can be found in some reported HP1 family-interacting proteins, as well as in the HP1 chromo shadow domain itself. Importantly, self-dimerization of the chromo shadow domain in vitro is disrupted by a peptide based on the consensus motif.
    • Smothers J.F., Henikoff S. The HP1 chromo shadow domain binds a consensus peptide pentamer. Curr Biol. 10:2000;27-30. By probing a random phage display library with a Drosophila HP1 chromo shadow domain, the authors identify a consensus peptide motif sufficient for chromo shadow domain binding. Sequences highly related to this consensus can be found in some reported HP1 family-interacting proteins, as well as in the HP1 chromo shadow domain itself. Importantly, self-dimerization of the chromo shadow domain in vitro is disrupted by a peptide based on the consensus motif.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.