scholarly journals The Origin Recognition Complex Functions in Sister-Chromatid Cohesion in Saccharomyces cerevisiae

Cell ◽  
2007 ◽  
Vol 128 (1) ◽  
pp. 85-99 ◽  
Author(s):  
Kenji Shimada ◽  
Susan M. Gasser
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Sister Chromatid ◽  
Origin Recognition Complex ◽  
Sister Chromatid Cohesion ◽  
Chromatid Cohesion ◽  
Complex Functions ◽  
Origin Recognition

scholarly journals Saccharomyces cerevisiae DNA Polymerase ε and Polymerase σ Interact Physically and Functionally, Suggesting a Role for Polymerase ε in Sister Chromatid Cohesion

2003 ◽  
Vol 23 (8) ◽  
pp. 2733-2748 ◽  
Author(s):  
Shaune Edwards ◽  
Caroline M. Li ◽  
Daniel L. Levy ◽  
Jessica Brown ◽  
Peter M. Snow ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Dna Polymerase ◽  
Sister Chromatid ◽  
Large Subunit ◽  
Polymerase Activity ◽  
Sister Chromatid Cohesion ◽  
Nucleotidyl Transferase ◽  
C Terminus ◽  
Chromatid Cohesion ◽  
A Subunit

ABSTRACT The large subunit of Saccharomyces cerevisiae DNA polymerase ε, Pol2, comprises two essential functions. The N terminus has essential DNA polymerase activity. The C terminus is also essential, but its function is unknown. We report here that the C-terminal domain of Pol2 interacts with polymerase σ (Pol σ), a recently identified, essential nuclear nucleotidyl transferase encoded by two redundant genes, TRF4 and TRF5. This interaction is functional, since Pol σ stimulates the polymerase activity of the Pol ε holoenzyme significantly. Since Trf4 is required for sister chromatid cohesion as well as for completion of S phase and repair, the interaction suggested that Pol ε, like Pol σ, might form a link between the replication apparatus and sister chromatid cohesion and/or repair machinery. We present evidence that pol2 mutants are defective in sister chromatid cohesion. In addition, Pol2 interacts with SMC1, a subunit of the cohesin complex, and with ECO1/CTF7, required for establishing sister chromatid cohesion; and pol2 mutations act synergistically with smc1 and scc1. We also show that trf5Δ mutants, like trf4Δ mutants, are defective in DNA repair and sister chromatid cohesion.

scholarly journals Drosophila Nipped-B Protein Supports Sister Chromatid Cohesion and Opposes the Stromalin/Scc3 Cohesion Factor To Facilitate Long-Range Activation of the cut Gene

2004 ◽  
Vol 24 (8) ◽  
pp. 3100-3111 ◽  
Author(s):  
Robert A. Rollins ◽  
Maria Korom ◽  
Nathalie Aulner ◽  
Andrew Martens ◽  
Dale Dorsett
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Drosophila Melanogaster ◽  
Long Range ◽  
Sister Chromatid ◽  
Transcriptional Activation ◽  
Domain Boundary ◽  
Sister Chromatid Cohesion ◽  
Chromatin Domain ◽  
Chromatid Cohesion ◽  
Evolutionarily Conserved

ABSTRACT The Drosophila melanogaster Nipped-B protein facilitates transcriptional activation of the cut and Ultrabithorax genes by remote enhancers. Sequence homologues of Nipped-B, Scc2 of Saccharomyces cerevisiae, and Mis4 of Schizosaccharomyces pombe are required for sister chromatid cohesion during mitosis. The evolutionarily conserved Cohesin protein complex mediates sister chromatid cohesion, and Scc2 and Mis4 are needed for Cohesin to associate with chromosomes. Here, we show that Nipped-B is also required for sister chromatid cohesion but that, opposite to the effect of Nipped-B, the stromalin/Scc3 component of Cohesin inhibits long-range activation of cut. To explain these findings, we propose a model based on the chromatin domain boundary activities of Cohesin in which Nipped-B facilitates cut activation by alleviating Cohesin-mediated blocking of enhancer-promoter communication.

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