Establishment of sister chromatid cohesion at the S. cerevisiae replication fork

Armelle Lengronne; John McIntyre; Yuki Katou; Yutaka Kanoh; Karl-Peter Hopfner; Katsuhiko Shirahige; Frank Uhlmann

doi:10.1016/j.molcel.2006.08.018

Establishment of sister chromatid cohesion at the S. cerevisiae replication fork

Mol Cell. 2006 Sep 15;23(6):787-99. doi: 10.1016/j.molcel.2006.08.018. Epub 2006 Sep 7.

Authors

Armelle Lengronne¹, John McIntyre, Yuki Katou, Yutaka Kanoh, Karl-Peter Hopfner, Katsuhiko Shirahige, Frank Uhlmann

Affiliation

¹ Chromosome Segregation Laboratory, Cancer Research UK London Research Institute, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London WC2A 3PX, United Kingdom.

PMID: 16962805
DOI: 10.1016/j.molcel.2006.08.018

Abstract

Two identical sister copies of eukaryotic chromosomes are synthesized during S phase. To facilitate their recognition as pairs for segregation in mitosis, sister chromatids are held together from their synthesis onward by the chromosomal cohesin complex. Replication fork progression is thought to be coupled to establishment of sister chromatid cohesion, facilitating identification of replication products, but evidence for this has remained circumstantial. Here we show that three proteins required for sister chromatid cohesion, Eco1, Ctf4, and Ctf18, are found at, and Ctf4 travels along chromosomes with, replication forks. The ring-shaped cohesin complex is loaded onto chromosomes before S phase in an ATP hydrolysis-dependent reaction. Cohesion establishment during DNA replication follows without further cohesin recruitment and without need for cohesin to re-engage an ATP hydrolysis motif that is critical for its initial DNA binding. This provides evidence for cohesion establishment in the context of replication forks and imposes constraints on the mechanism involved.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Acetyltransferases / analysis
Acetyltransferases / metabolism
Acetyltransferases / physiology
Adenosine Triphosphatases / chemistry
Adenosine Triphosphatases / metabolism
Amino Acid Motifs / physiology
Cell Cycle Proteins / analysis
Cell Cycle Proteins / metabolism
Chromatids / metabolism*
Chromosomal Proteins, Non-Histone / analysis
Chromosomal Proteins, Non-Histone / metabolism
Cohesins
DNA Replication / physiology*
DNA, Fungal / biosynthesis
DNA-Binding Proteins / analysis
DNA-Binding Proteins / metabolism
DNA-Binding Proteins / physiology
Models, Genetic
Nuclear Proteins / analysis
Nuclear Proteins / metabolism
Nuclear Proteins / physiology
Proliferating Cell Nuclear Antigen / metabolism
S Phase / physiology
Saccharomyces cerevisiae / genetics*
Saccharomyces cerevisiae / metabolism
Saccharomyces cerevisiae Proteins / analysis
Saccharomyces cerevisiae Proteins / metabolism
Saccharomyces cerevisiae Proteins / physiology

Substances

CTF18 protein, S cerevisiae
CTF4 protein, S cerevisiae
Cell Cycle Proteins
Chromosomal Proteins, Non-Histone
DNA, Fungal
DNA-Binding Proteins
Nuclear Proteins
Proliferating Cell Nuclear Antigen
Saccharomyces cerevisiae Proteins
Acetyltransferases
ECO1 protein, S cerevisiae
Adenosine Triphosphatases

Associated data

OMIM/GSE5719