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 ◽  
...  

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.

2011 ◽  
Vol 22 (8) ◽  
pp. 1181-1190 ◽  
Author(s):  
Jungseog Kang ◽  
Jaideep Chaudhary ◽  
Hui Dong ◽  
Soonjoung Kim ◽  
Chad A. Brautigam ◽  
...  

Human Shugoshin 1 (Sgo1) protects centromeric sister-chromatid cohesion during prophase and prevents premature sister-chromatid separation. Heterochromatin protein 1 (HP1) has been proposed to protect centromeric sister-chromatid cohesion by directly targeting Sgo1 to centromeres in mitosis. Here we show that HP1α is targeted to mitotic centromeres by INCENP, a subunit of the chromosome passenger complex (CPC). Biochemical and structural studies show that both HP1–INCENP and HP1–Sgo1 interactions require the binding of the HP1 chromo shadow domain to PXVXL/I motifs in INCENP or Sgo1, suggesting that the INCENP-bound, centromeric HP1α is incapable of recruiting Sgo1. Consistently, a Sgo1 mutant deficient in HP1 binding is functional in centromeric cohesion protection and localizes normally to centromeres in mitosis. By contrast, INCENP or Sgo1 mutants deficient in HP1 binding fail to localize to centromeres in interphase. Therefore, our results suggest that HP1 binding by INCENP or Sgo1 is dispensable for centromeric cohesion protection during mitosis of human cells, but might regulate yet uncharacterized interphase functions of CPC or Sgo1 at the centromeres.


2001 ◽  
Vol 276 (46) ◽  
pp. 42857-42862 ◽  
Author(s):  
Amy C. Madril ◽  
Robert E. Johnson ◽  
M. Todd Washington ◽  
Louise Prakash ◽  
Satya Prakash

2004 ◽  
Vol 24 (8) ◽  
pp. 3100-3111 ◽  
Author(s):  
Robert A. Rollins ◽  
Maria Korom ◽  
Nathalie Aulner ◽  
Andrew Martens ◽  
Dale Dorsett

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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