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MBC in Press, published online ahead of print June 15, 2005
Mol. Biol. Cell 10.1091/mbc.E04-12-1063

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Submitted on December 10, 2004
Revised on May 23, 2005
Accepted on June 3, 2005

Two Human Orthologues of Eco1/Ctf7 Acetyltransferases Are Both Required for Proper Sister-Chromatid Cohesion

Fajian Hou and Hui Zou

Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9148

Monitoring Editor: Orna Cohen-Fix

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 as 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 auto-acetylation reaction in vitro. However, no similarity can be detected outside of the conserved domain. RNAi depletion experiment revealed that EFO1/ESCO1 and EFO2/ESCO2 were not redundant and both were required for proper sister-chromatid cohesion. The difference between EFO1 and EFO2 is also reflected in their cell cycle regulation. In mitosis, EFO1 is phosphorylated while as 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.


Address correspondence to: Hui Zou (hui.zou{at}utsouthwestern.edu)




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