Interaction between the Drosophila CAF-1 and ASF1 chromatin assembly factors.

TitleInteraction between the Drosophila CAF-1 and ASF1 chromatin assembly factors.
Publication TypeJournal Article
Year of Publication2001
AuthorsTyler JK, Collins KA, Prasad-Sinha J, Amiott E, Bulger M, Harte PJ, Kobayashi R, Kadonaga JT
JournalMol Cell Biol
Date Published2001 Oct
KeywordsAnimals, Cell Cycle Proteins, Chromatin, Chromatin Assembly Factor-1, Chromosomal Proteins, Non-Histone, Cloning, Molecular, DNA-Binding Proteins, Drosophila, Drosophila Proteins, Microscopy, Fluorescence, Molecular Chaperones, Molecular Sequence Data, Nuclear Proteins, Peptides, Protein Subunits, Retinoblastoma-Binding Protein 4, Sequence Homology, Amino Acid, Spodoptera, Transfection

The assembly of newly synthesized DNA into chromatin is essential for normal growth, development, and differentiation. To gain a better understanding of the assembly of chromatin during DNA synthesis, we identified, cloned, and characterized the 180- and 105-kDa polypeptides of Drosophila chromatin assembly factor 1 (dCAF-1). The purified recombinant p180+p105+p55 dCAF-1 complex is active for DNA replication-coupled chromatin assembly. Furthermore, we have established that the putative 75-kDa polypeptide of dCAF-1 is a C-terminally truncated form of p105 that does not coexist in dCAF-1 complexes containing the p105 subunit. The analysis of native and recombinant dCAF-1 revealed an interaction between dCAF-1 and the Drosophila anti-silencing function 1 (dASF1) component of replication-coupling assembly factor (RCAF). The binding of dASF1 to dCAF-1 is mediated through the p105 subunit of dCAF-1. Consistent with the interaction between dCAF-1 p105 and dASF1 in vitro, we observed that dASF1 and dCAF-1 p105 colocalized in vivo in Drosophila polytene chromosomes. This interaction between dCAF-1 and dASF1 may be a key component of the functional synergy observed between RCAF and dCAF-1 during the assembly of newly synthesized DNA into chromatin.

Alternate JournalMol Cell Biol
PubMed ID11533245
PubMed Central IDPMC99803
Grant ListR01 GM058272 / GM / NIGMS NIH HHS / United States
GM58272 / GM / NIGMS NIH HHS / United States
Related Faculty: 
Jessica K. Tyler, Ph.D.

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