Two human orthologues of Eco1/Ctf7 acetyltransferases are both required for proper sister-chromatid cohesion

Mol Biol Cell. 2005 Aug;16(8):3908-18. doi: 10.1091/mbc.e04-12-1063. Epub 2005 Jun 15.


Genetic studies in yeast and Drosophila have uncovered a conserved acetyltransferase involved in sister-chromatid cohesion. Here, we described the two human orthologues, previously named EFO1/ESCO1 and EFO2/ESCO2. Similar to their yeast (Eco1/Ctf7 and Eso1) and fly (deco) counterparts, both proteins feature a conserved C-terminal domain consisting of a H2C2 zinc finger motif and an acetyltransferase domain that is able to catalyze autoacetylation reaction in vitro. However, no similarity can be detected outside of the conserved domain. RNA interference depletion experiment revealed that EFO1/ESCO1 and EFO2/ESCO2 were not redundant and that both were required for proper sister-chromatid cohesion. The difference between EFO1 and EFO2 also is reflected in their cell cycle regulation. In mitosis, EFO1 is phosphorylated, whereas EFO2 is degraded. Furthermore, both proteins associate with chromosomes, and the chromosome binding depends on the diverse N-terminal domains. We propose that EFO1 and EFO2 are targeted to different chromosome structures to help establish or maintain sister-chromatid cohesion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetyltransferases / chemistry
  • Acetyltransferases / genetics
  • Acetyltransferases / metabolism*
  • Amino Acid Sequence
  • Cell Cycle
  • Cell Cycle Proteins / metabolism
  • Cells, Cultured
  • Chromatids / metabolism*
  • Chromosomal Proteins, Non-Histone / chemistry
  • Chromosomal Proteins, Non-Histone / genetics
  • Chromosomal Proteins, Non-Histone / metabolism*
  • Chromosome Pairing*
  • Chromosome Segregation
  • Cohesins
  • Fungal Proteins / metabolism
  • Humans
  • Molecular Sequence Data
  • Nuclear Proteins / metabolism
  • Phosphoproteins
  • Protein Binding
  • RNA, Small Interfering / genetics
  • RNA, Small Interfering / metabolism
  • Saccharomyces cerevisiae Proteins
  • Sequence Alignment


  • Cell Cycle Proteins
  • Chromosomal Proteins, Non-Histone
  • Fungal Proteins
  • MCD1 protein, S cerevisiae
  • Nuclear Proteins
  • Phosphoproteins
  • RNA, Small Interfering
  • Saccharomyces cerevisiae Proteins
  • Acetyltransferases
  • ESCO1 protein, human
  • ESCO2 protein, human