Journal article
Does heterochromatin protein 1 always follow code?
Proceedings of the National Academy of Sciences - PNAS, Vol.99(Suppl 4), pp.16462-16469
Colloquium Paper
12/10/2002
DOI: 10.1073/pnas.162371699
PMCID: PMC139909
PMID: 12151603
Abstract
Heterochromatin protein 1 (HP1) is a conserved chromosomal protein that participates in chromatin packaging and gene silencing. A loss of HP1 leads to lethality in
Drosophila
and correlates with metastasis in human breast cancer cells. On
Drosophila
polytene chromosomes HP1 is localized to centric regions, telomeric regions, in a banded pattern along the fourth chromosome, and at many sites scattered throughout the euchromatic arms. Recently, one mechanism of HP1 chromosome association was revealed; the amino-terminal chromo domain of HP1 interacts with methylated lysine nine of histone H3, consistent with the histone code hypothesis. Compelling data support this mechanism of HP1 association at centric regions. Is this the only mechanism by which HP1 associates with chromosomes? Interest is now shifting toward the role of HP1 within euchromatic domains. Accumulating evidence in
Drosophila
and mammals suggests that HP1 associates with chromosomes through interactions with nonhistone chromosomal proteins at locations other than centric heterochromatin. Does HP1 play a similar role in chromatin packaging and gene regulation at these sites as it does in centric heterochromatin? Does HP1 associate with the same proteins at these sites as it does in centric heterochromatin? A first step toward answering these questions is the identification of sequences associated with HP1 within euchromatic domains. Such sequences are likely to include HP1 “target genes” whose discovery will aid in our understanding of HP1 lethality in
Drosophila
and metastasis of breast cancer cells.
Details
- Title: Subtitle
- Does heterochromatin protein 1 always follow code?
- Creators
- Yuhong Li - Departments ofDawn A Kirschmann - Departments ofLori L Wallrath - Departments of
- Resource Type
- Journal article
- Publication Details
- Proceedings of the National Academy of Sciences - PNAS, Vol.99(Suppl 4), pp.16462-16469
- Publisher
- The National Academy of Sciences
- Series
- Colloquium Paper
- DOI
- 10.1073/pnas.162371699
- PMID
- 12151603
- PMCID
- PMC139909
- ISSN
- 0027-8424
- eISSN
- 1091-6490
- Language
- English
- Date published
- 12/10/2002
- Academic Unit
- Biochemistry and Molecular Biology; University College Courses
- Record Identifier
- 9984025279002771
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