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PMID: 8421049 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Overlapping domains of the heterochromatin-associated protein HP1 mediate nuclear localization and heterochromatin binding.

The Journal of cell biology ·Vol. 120 ·No. 2 ·1993-01-00 ·Pages 291-9

Powers JA, Eissenberg JC

Abstract

The Drosophila protein HP1 is a 206 amino acid heterochromatin-associated nonhistone chromosomal protein. Based on the characterization of HP1 to date, there are three properties intrinsic to HP1: nuclear localization, heterochromatin binding, and gene silencing. In this work, we have concentrated on the identification of domains responsible for the nuclear localization and heterochromatin binding properties of HP1. We have expressed a series of beta-galactosidase/HP1 fusion proteins in Drosophila embryos and polytene tissue and have used beta-galactosidase enzymatic activity to identify the subcellular localization of each fusion protein. We have identified two functional domains in HP1: a nuclear localization domain of amino acids 152-206 and a heterochromatin binding domain of amino acids 95-206. Both of these functional domains overlap an evolutionarily conserved COOH-terminal region.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Binding Sites Biological Evolution Cell Nucleus/metabolism,ultrastructure Chromobox Protein Homolog 5 Chromosomal Proteins, Non-Histone/genetics,metabolism Drosophila melanogaster/metabolism Fluorescent Antibody Technique Heterochromatin/metabolism,ultrastructure Molecular Sequence Data Mutagenesis, Site-Directed Oligodeoxyribonucleotides Plasmids Polymerase Chain Reaction/methods Recombinant Fusion Proteins/metabolism Sequence Homology, Amino Acid beta-Galactosidase/metabolism
Chemicals
Chromosomal Proteins, Non-Histone Heterochromatin Oligodeoxyribonucleotides Recombinant Fusion Proteins Chromobox Protein Homolog 5 beta-Galactosidase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Powers J A
Edward A. Doisy Department of Biochemistry and Molecular Biology, St. Louis University School of Medicine, Missouri 63104.
Eissenberg J C
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.120.2.291
Published
1993-01-00
Pages
291-9
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2119527
Subset
IM
Grants
NIGMS NIH HHS · GM 40732 · United States
External Links
PubMed source DOI: 10.1083/jcb.120.2.291 PMC Full Text View journal details
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