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| Content Provider | PubMed Central |
|---|---|
| Author | Stephens, Gena E. Xiao, Hua Lankenau, Dirk-h. Wu, Carl Elgin, Sarah C. R. |
| Abstract | Heterochromatin Protein 2 is a nonhistone chromosomal protein from Drosophila melanogaster that binds to HP1 and has been implicated in heterochromatin-induced gene silencing. Heretofore, HP1 has been the only known binding partner of HP2, a large protein devoid of sequence motifs other than a pair of AT-hooks. In an effort to identify proteins that interact with HP2 and assign functions to its various domains, nuclear proteins were fractionated under non-denaturing conditions. On separation of nuclear proteins, Nap-1, or Nucleosome assembly protein 1, has an overlapping elution profile with HP2 (assayed by Western blot) and has been identified by mass spectrometry in fractions with HP2. Upon probing fractions in which HP2 and Nap-1 are both present, we find that NURF, an ISWI-dependent chromatin remodeling complex, is also present. Results from coimmunoprecipitation experiments suggest that HP2 interacts with Nap-1 as well as with NURF; NURF appears to interact directly with both HP2 and Nap-1. Three distinct domains within HP2 mediate the interaction with NURF, allowing us to assign NURF binding domains in addition to the AT-hooks and HP1 binding domains already mapped in HP2. Mutations in Nap-1 are shown to suppress position effect variegation, suggesting that Nap-1 functions to help assemble chromatin into a closed form, as does HP2. Based on these interactions, we speculate that HP2 may cooperate with these factors in the remodeling of chromatin for silencing. |
| Related Links | http://dx.doi.org/10.1021/bi060983y |
| Ending Page | 14999 |
| Page Count | 10 |
| Starting Page | 14990 |
| File Format | |
| ISSN | 00062960 |
| e-ISSN | 15204995 |
| Journal | Biochemistry |
| Issue Number | 50 |
| Volume Number | 45 |
| Language | English |
| Publisher Date | 2006-12-01 |
| Access Restriction | Open |
| Subject Keyword | Biochemistry Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry |
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