Current Genetics

, Volume 57, Issue 4, pp 271–286

Genetic interactions between POB3 and the acetylation of newly synthesized histones

  • Devi M. Nair
  • Zhongqi Ge
  • Erica L. Mersfelder
  • Mark R. Parthun
Research Article

DOI: 10.1007/s00294-011-0347-1

Cite this article as:
Nair, D.M., Ge, Z., Mersfelder, E.L. et al. Curr Genet (2011) 57: 271. doi:10.1007/s00294-011-0347-1

Abstract

Pob3p is an essential component of the S. cerevisiae FACT complex (yFACT). Several lines of evidence indicate that the yFACT complex plays an important role in chromatin assembly including the observation that the pob3 Q308K allele is synthetically lethal with an allele of histone H4 that prevents the diacetylation of newly synthesized molecules. We have analyzed the genetic interactions between the Q308K allele of POB3 and mutations in all of the sites of acetylation that have been identified on newly synthesized histones. Genetic interactions were observed between POB3 and sites of acetylation on the NH2-terminal tails of H3 and H4. For histone H3, lysine residues 14 and 23 were particularly important when POB3 activity is compromised. Surprisingly, synthetic defects observed when the pob3 Q308K allele was combined with mutations of H4 lysines 5 and 12, were not phenocopied by deletion of HAT1, which encodes the enzyme that is thought to generate this pattern of acetylation on H4. Genetic interactions were also observed between POB3 and sites of acetylation found in the core domain of newly synthesized histones H3 and H4. These include synthetic lethality with an allele of H4 lysine 91 that mimics constitutive acetylation. While the mutations that alter H4 lysines 5, 12 and 91 do not affect binding to Pob3p, mutation of histone H3 lysine 56 decreases the association of histones with Pob3p. These results support the model that the yFACT complex plays a central role in chromatin assembly pathways regulated by acetylation of newly synthesized histones.

Keywords

ChromatinChromatin assemblyHistoneHistone chaperoneHistone acetylationFACT complexHAT1

Supplementary material

294_2011_347_MOESM1_ESM.pdf (5.5 mb)
Supplemental Figures (PDF 5,655 kb)

Copyright information

© Springer-Verlag 2011

Authors and Affiliations

  • Devi M. Nair
    • 1
  • Zhongqi Ge
    • 1
  • Erica L. Mersfelder
    • 1
  • Mark R. Parthun
    • 1
  1. 1.Department of Molecular and Cellular BiochemistryThe Ohio State UniversityColumbusUSA