Functional conservation and specialization among eukaryotic anti-silencing function 1 histone chaperones. Academic Article uri icon

Overview

abstract

  • Chromatin disassembly and reassembly, mediated by histone chaperones such as anti-silencing function 1 (Asf1), are likely to accompany all nuclear processes that occur on the DNA template. In order to gain insight into the functional conservation of Asf1 across eukaryotes, we have replaced the budding yeast Asf1 protein with Drosophila Asf1 (dAsf1) or either of the two human Asf1 (hAsf1a and hAsf1b) counterparts. We found that hAsf1b is best able to rescue the growth defect of Saccharomyces cerevisiae lacking Asf1. Moreover, dAsf1 and hAsf1b but not hAsf1a can replace the role of yeast Asf1 in protecting against replicational stress and activating the PHO5 gene, while only hAsf1a can replace the role of Asf1 in protecting against double-stranded-DNA-damaging agents. Furthermore, it appears that the interaction between Asf1 and the DNA damage checkpoint protein Rad53 is not required for Asf1's role in maintaining genomic integrity. In addition to indicating the functional conservation of the Asf1 proteins across species, these studies suggest distinct roles for the two human Asf1 proteins.

publication date

  • September 1, 2005

Research

keywords

  • Cell Cycle Proteins
  • Gene Silencing
  • Histones
  • Molecular Chaperones
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins

Identity

PubMed Central ID

  • PMC1214205

Scopus Document Identifier

  • 25144465002

Digital Object Identifier (DOI)

  • 10.1128/EC.4.9.1583-1590.2005

PubMed ID

  • 16151251

Additional Document Info

volume

  • 4

issue

  • 9