Analysis of the heterochromatin protein 1 (HP1) interactome in Drosophila

Hyun Wook Ryu, Dong Hoon Lee, Laurence Florens, Selene K. Swanson, Michael P. Washburn, So Hee Kwon

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Heterochromatin protein 1 (HP1) was first described in Drosophila melanogaster as a heterochromatin associated protein required for epigenetic gene silencing. Most eukaryotes have at least three HP1 homologs that play differential roles in heterochromatin and euchromatin. However, despite the fact that the three HP1 proteins bind to different regions of the genome, several studies show that most of the interactions occur in a manner specific to HP1a. In addition, little is known about the overall interaction network of the three Drosophila HP1 homologs, HP1a, HP1b, and HP1c. Here, we performed the first comprehensive proteomic analysis of Drosophila HP1 homologs by coupling a double-affinity purification approach with MudPIT analysis to identify interacting proteins of Drosophila HP1. We discovered 160-310 proteins co-eluted with HP1, including a number of novel HP1-binding partners along with the previously identified HP1 binding proteins. Finally, we showed that slight and unique binding preferences might exist between the three HP1 proteins in Drosophila. These studies are the first to systematically analyze the interactome of HP1 paralogs and provide the basic clues as to the molecular mechanism by which HP1 might control cellular processes. Biological significance: Most eukaryotes have at least three HP1 homologs with similar domain structures but with differential roles in heterochromatin and euchromatin. However, little is known about the overall interactome of the three Drosophila HP1 homologs, HP1a, HP1b, and HP1c. The present study compared interacting proteins of three HP1 homologs in Drosophila. To better understand the underlying mechanisms for gene regulation of HP1, a double-affinity purification and MudPIT mass spectrometry were employed to identify differential proteins as well as common binding proteins of HP1. Therefore, this study provides not only the comparative proteomic analysis but also molecular mechanism underlying the HP1 homolog-specific function.

Original languageEnglish
Pages (from-to)137-147
Number of pages11
JournalJournal of Proteomics
Volume102
DOIs
Publication statusPublished - 2014 May 6

Fingerprint

Drosophila
Heterochromatin
Euchromatin
Proteins
heterochromatin-specific nonhistone chromosomal protein HP-1
Eukaryota
Protein Binding
Proteomics
Purification
Carrier Proteins
Genes
Gene Silencing
Drosophila melanogaster
Epigenomics
Gene expression
Mass spectrometry
Mass Spectrometry
Genome

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Medicine(all)

Cite this

Ryu, Hyun Wook ; Lee, Dong Hoon ; Florens, Laurence ; Swanson, Selene K. ; Washburn, Michael P. ; Kwon, So Hee. / Analysis of the heterochromatin protein 1 (HP1) interactome in Drosophila. In: Journal of Proteomics. 2014 ; Vol. 102. pp. 137-147.
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abstract = "Heterochromatin protein 1 (HP1) was first described in Drosophila melanogaster as a heterochromatin associated protein required for epigenetic gene silencing. Most eukaryotes have at least three HP1 homologs that play differential roles in heterochromatin and euchromatin. However, despite the fact that the three HP1 proteins bind to different regions of the genome, several studies show that most of the interactions occur in a manner specific to HP1a. In addition, little is known about the overall interaction network of the three Drosophila HP1 homologs, HP1a, HP1b, and HP1c. Here, we performed the first comprehensive proteomic analysis of Drosophila HP1 homologs by coupling a double-affinity purification approach with MudPIT analysis to identify interacting proteins of Drosophila HP1. We discovered 160-310 proteins co-eluted with HP1, including a number of novel HP1-binding partners along with the previously identified HP1 binding proteins. Finally, we showed that slight and unique binding preferences might exist between the three HP1 proteins in Drosophila. These studies are the first to systematically analyze the interactome of HP1 paralogs and provide the basic clues as to the molecular mechanism by which HP1 might control cellular processes. Biological significance: Most eukaryotes have at least three HP1 homologs with similar domain structures but with differential roles in heterochromatin and euchromatin. However, little is known about the overall interactome of the three Drosophila HP1 homologs, HP1a, HP1b, and HP1c. The present study compared interacting proteins of three HP1 homologs in Drosophila. To better understand the underlying mechanisms for gene regulation of HP1, a double-affinity purification and MudPIT mass spectrometry were employed to identify differential proteins as well as common binding proteins of HP1. Therefore, this study provides not only the comparative proteomic analysis but also molecular mechanism underlying the HP1 homolog-specific function.",
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Analysis of the heterochromatin protein 1 (HP1) interactome in Drosophila. / Ryu, Hyun Wook; Lee, Dong Hoon; Florens, Laurence; Swanson, Selene K.; Washburn, Michael P.; Kwon, So Hee.

In: Journal of Proteomics, Vol. 102, 06.05.2014, p. 137-147.

Research output: Contribution to journalArticle

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