The Amino-Terminal TPR Domain of Dia2 Tethers SCFDia2 to the Replisome Progression Complex
Eukaryotic cells contain multiple versions of the E3 ubiquitin ligase known as the SCF (Skp1/cullin/F box), each of which is distinguished by a different F box protein that uses a domain at the carboxyl terminus to recognize substrates [1, 2]. The F box protein Dia2 is an important determinant of ge...
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Published in | Current biology Vol. 19; no. 22; pp. 1943 - 1949 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
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01.12.2009
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ISSN | 0960-9822 1879-0445 |
DOI | 10.1016/j.cub.2009.09.062 |
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Abstract | Eukaryotic cells contain multiple versions of the E3 ubiquitin ligase known as the SCF (Skp1/cullin/F box), each of which is distinguished by a different F box protein that uses a domain at the carboxyl terminus to recognize substrates [1, 2]. The F box protein Dia2 is an important determinant of genome stability in budding yeast [3–5], but its mode of action is poorly understood. Here we show that SCFDia2 associates with the replisome progression complex (RPC) that assembles around the MCM2-7 helicase at DNA replication forks [6]. This interaction requires the RPC components Mrc1 and Ctf4, both of which associate with a tetratricopeptide repeat (TPR) domain located at the amino terminus of Dia2. Our data indicate that the TPR domain of Dia2 tethers SCFDia2 to the RPC, probably increasing the local concentration of the ligase at DNA replication forks. This regulation becomes important in cells that accumulate stalled DNA replication forks at protein-DNA barriers, perhaps aiding the interaction of SCFDia2 with key substrates. Our findings suggest that the amino-terminal domains of other F box proteins might also play an analogous regulatory role, controlling the localization of the cognate SCF complexes. |
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AbstractList | Eukaryotic cells contain multiple versions of the E3 ubiquitin ligase known as the SCF (Skp1/cullin/F box), each of which is distinguished by a different F box protein that uses a domain at the carboxyl terminus to recognize substrates [1, 2]. The F box protein Dia2 is an important determinant of genome stability in budding yeast [3–5], but its mode of action is poorly understood. Here we show that SCFDia2 associates with the replisome progression complex (RPC) that assembles around the MCM2-7 helicase at DNA replication forks [6]. This interaction requires the RPC components Mrc1 and Ctf4, both of which associate with a tetratricopeptide repeat (TPR) domain located at the amino terminus of Dia2. Our data indicate that the TPR domain of Dia2 tethers SCFDia2 to the RPC, probably increasing the local concentration of the ligase at DNA replication forks. This regulation becomes important in cells that accumulate stalled DNA replication forks at protein-DNA barriers, perhaps aiding the interaction of SCFDia2 with key substrates. Our findings suggest that the amino-terminal domains of other F box proteins might also play an analogous regulatory role, controlling the localization of the cognate SCF complexes. |
Author | Labib, Karim Maculins, Timurs Morohashi, Hiroko |
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Cites_doi | 10.1016/j.molcel.2005.06.037 10.1016/j.jmb.2005.01.041 10.1128/MCB.24.9.4019-4031.2004 10.1126/science.1146994 10.1016/j.molcel.2008.08.020 10.1073/pnas.0506540103 10.1038/nature01692 10.1038/nature01900 10.1042/BST0370495 10.1091/mbc.E03-08-0619 10.1016/j.molcel.2005.07.028 10.1016/j.cell.2007.04.042 10.1073/pnas.0608566103 10.1038/emboj.2009.226 10.1074/jbc.M308875200 10.1091/mbc.E05-09-0884 10.1016/j.tibs.2009.01.010 10.1534/genetics.106.057836 10.1038/ncb1382 10.1016/S1097-2765(03)00456-8 10.1534/genetics.107.072876 10.1101/gad.982902 10.1093/emboj/16.19.5966 10.1038/nature06132 10.1128/MCB.21.15.4938-4948.2001 10.1038/nrm1471 10.1016/j.bbamcr.2004.09.027 10.1101/gad.337205 10.1371/journal.pgen.0030228 10.1016/j.cell.2005.12.036 10.1128/MCB.12.9.4056 |
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References | Blake, Luke, Kanellis, Jorgensen, Goh, Penfold, Breitkreutz, Durocher, Peter, Tyers (bib3) 2006; 174 Pan, Ye, Yuan, Wang, Bader, Boeke (bib5) 2006; 124 Drury, Perkins, Diffley (bib17) 1997; 16 Brunson, Dixon, Kozubowski, Mathias (bib27) 2004; 279 Kanemaki, Sanchez-Diaz, Gambus, Labib (bib31) 2003; 423 Gambus, Jones, Sanchez-Diaz, Kanemaki, van Deursen, Edmondson, Labib (bib6) 2006; 8 Tourrière, Versini, Cordón-Preciado, Alabert, Pasero (bib10) 2005; 19 Alvaro, Lisby, Rothstein (bib26) 2007; 3 Katou, Kanoh, Bando, Noguchi, Tanaka, Ashikari, Sugimoto, Shirahige (bib13) 2003; 424 Cardozo, Pagano (bib1) 2004; 5 Gambus, van Deursen, Polychronopoulos, Foltman, Jones, Edmondson, Calzada, Labib (bib15) 2009; 28 Tang, Orlicky, Lin, Willems, Neculai, Ceccarelli, Mercurio, Shilton, Sicheri, Tyers (bib28) 2007; 129 Mayer, Pot, Chang, Xu, Aneliunas, Kwok, Newitt, Aebersold, Boone, Brown, Hieter (bib11) 2004; 15 Koepp, Kile, Swaminathan, Rodriguez-Rivera (bib4) 2006; 17 Szyjka, Viggiani, Aparicio (bib9) 2005; 19 Wang, Vujcic, Kowalski (bib23) 2001; 21 Nedelcheva, Roguev, Dolapchiev, Shevchenko, Taskov, Shevchenko, Stewart, Stoynov (bib12) 2005; 347 Sawa, Nusinow, Kay, Imaizumi (bib30) 2007; 318 Ivessa, Lenzmeier, Bessler, Goudsouzian, Schnakenberg, Zakian (bib24) 2003; 12 Mohanty, Bairwa, Bastia (bib8) 2006; 103 Xu, Boone, Brown (bib14) 2007; 176 Ivessa, Zhou, Schulz, Monson, Zakian (bib21) 2002; 16 Makovets, Herskowitz, Blackburn (bib22) 2004; 24 Mimitou, Symington (bib18) 2009; 34 Willems, Schwab, Tyers (bib2) 2004; 1695 Lou, Komata, Katou, Guan, Reis, Budd, Shirahige, Campbell (bib16) 2008; 32 Calzada, Hodgson, Kanemaki, Bueno, Labib (bib7) 2005; 19 Greenfeder, Newlon (bib20) 1992; 12 Kim, Fujiwara, Suh, Kim, Kim, Han, David, Putterill, Nam, Somers (bib29) 2007; 449 Rouse (bib19) 2009; 37 Schmidt, Kolodner (bib25) 2006; 103 Tang (10.1016/j.cub.2009.09.062_bib28) 2007; 129 Brunson (10.1016/j.cub.2009.09.062_bib27) 2004; 279 Gambus (10.1016/j.cub.2009.09.062_bib6) 2006; 8 Ivessa (10.1016/j.cub.2009.09.062_bib24) 2003; 12 Tourrière (10.1016/j.cub.2009.09.062_bib10) 2005; 19 Greenfeder (10.1016/j.cub.2009.09.062_bib20) 1992; 12 Ivessa (10.1016/j.cub.2009.09.062_bib21) 2002; 16 Nedelcheva (10.1016/j.cub.2009.09.062_bib12) 2005; 347 Xu (10.1016/j.cub.2009.09.062_bib14) 2007; 176 Cardozo (10.1016/j.cub.2009.09.062_bib1) 2004; 5 Schmidt (10.1016/j.cub.2009.09.062_bib25) 2006; 103 Makovets (10.1016/j.cub.2009.09.062_bib22) 2004; 24 Mimitou (10.1016/j.cub.2009.09.062_bib18) 2009; 34 Mayer (10.1016/j.cub.2009.09.062_bib11) 2004; 15 Drury (10.1016/j.cub.2009.09.062_bib17) 1997; 16 Lou (10.1016/j.cub.2009.09.062_bib16) 2008; 32 Wang (10.1016/j.cub.2009.09.062_bib23) 2001; 21 Calzada (10.1016/j.cub.2009.09.062_bib7) 2005; 19 Willems (10.1016/j.cub.2009.09.062_bib2) 2004; 1695 Sawa (10.1016/j.cub.2009.09.062_bib30) 2007; 318 Pan (10.1016/j.cub.2009.09.062_bib5) 2006; 124 Koepp (10.1016/j.cub.2009.09.062_bib4) 2006; 17 Alvaro (10.1016/j.cub.2009.09.062_bib26) 2007; 3 Katou (10.1016/j.cub.2009.09.062_bib13) 2003; 424 Blake (10.1016/j.cub.2009.09.062_bib3) 2006; 174 Gambus (10.1016/j.cub.2009.09.062_bib15) 2009; 28 Kim (10.1016/j.cub.2009.09.062_bib29) 2007; 449 Szyjka (10.1016/j.cub.2009.09.062_bib9) 2005; 19 Kanemaki (10.1016/j.cub.2009.09.062_bib31) 2003; 423 Rouse (10.1016/j.cub.2009.09.062_bib19) 2009; 37 Mohanty (10.1016/j.cub.2009.09.062_bib8) 2006; 103 |
References_xml | – volume: 174 start-page: 1709 year: 2006 end-page: 1727 ident: bib3 article-title: The F-box protein Dia2 overcomes replication impedance to promote genome stability in Saccharomyces cerevisiae publication-title: Genetics – volume: 424 start-page: 1078 year: 2003 end-page: 1083 ident: bib13 article-title: S-phase checkpoint proteins Tof1 and Mrc1 form a stable replication-pausing complex publication-title: Nature – volume: 176 start-page: 1417 year: 2007 end-page: 1429 ident: bib14 article-title: Genetic dissection of parallel sister-chromatid cohesion pathways publication-title: Genetics – volume: 24 start-page: 4019 year: 2004 end-page: 4031 ident: bib22 article-title: Anatomy and dynamics of DNA replication fork movement in yeast telomeric regions publication-title: Mol. Cell. Biol. – volume: 32 start-page: 106 year: 2008 end-page: 117 ident: bib16 article-title: Mrc1 and DNA polymerase ɛ function together in linking DNA replication and the S phase checkpoint publication-title: Mol. Cell – volume: 103 start-page: 897 year: 2006 end-page: 902 ident: bib8 article-title: The Tof1p-Csm3p protein complex counteracts the Rrm3p helicase to control replication termination of Saccharomyces cerevisiae publication-title: Proc. Natl. Acad. Sci. USA – volume: 37 start-page: 495 year: 2009 end-page: 510 ident: bib19 article-title: Control of genome stability by SLX protein complexes publication-title: Biochem. Soc. Trans. – volume: 347 start-page: 509 year: 2005 end-page: 521 ident: bib12 article-title: Uncoupling of unwinding from DNA synthesis implies regulation of MCM helicase by Tof1/Mrc1/Csm3 checkpoint complex publication-title: J. Mol. Biol. – volume: 1695 start-page: 133 year: 2004 end-page: 170 ident: bib2 article-title: A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin publication-title: Biochim. Biophys. Acta – volume: 129 start-page: 1165 year: 2007 end-page: 1176 ident: bib28 article-title: Suprafacial orientation of the SCFCdc4 dimer accommodates multiple geometries for substrate ubiquitination publication-title: Cell – volume: 19 start-page: 1905 year: 2005 end-page: 1919 ident: bib7 article-title: Molecular anatomy and regulation of a stable replisome at a paused eukaryotic DNA replication fork publication-title: Genes Dev. – volume: 16 start-page: 5966 year: 1997 end-page: 5976 ident: bib17 article-title: The Cdc4/34/53 pathway targets Cdc6p for proteolysis in budding yeast publication-title: EMBO J. – volume: 12 start-page: 4056 year: 1992 end-page: 4066 ident: bib20 article-title: Replication forks pause at yeast centromeres publication-title: Mol. Cell. Biol. – volume: 8 start-page: 358 year: 2006 end-page: 366 ident: bib6 article-title: GINS maintains association of Cdc45 with MCM in replisome progression complexes at eukaryotic DNA replication forks publication-title: Nat. Cell Biol. – volume: 28 start-page: 2992 year: 2009 end-page: 3004 ident: bib15 article-title: A key role for Ctf4 in coupling the MCM2-7 helicase to DNA polymerase alpha within the eukaryotic replisome publication-title: EMBO J. – volume: 3 start-page: e228 year: 2007 ident: bib26 article-title: Genome-wide analysis of Rad52 foci reveals diverse mechanisms impacting recombination publication-title: PLoS Genet. – volume: 34 start-page: 264 year: 2009 end-page: 272 ident: bib18 article-title: Nucleases and helicases take center stage in homologous recombination publication-title: Trends Biochem. Sci. – volume: 17 start-page: 1540 year: 2006 end-page: 1548 ident: bib4 article-title: The F-box protein Dia2 regulates DNA replication publication-title: Mol. Biol. Cell – volume: 318 start-page: 261 year: 2007 end-page: 265 ident: bib30 article-title: FKF1 and GIGANTEA complex formation is required for day-length measurement in Arabidopsis publication-title: Science – volume: 16 start-page: 1383 year: 2002 end-page: 1396 ident: bib21 article-title: Saccharomyces Rrm3p, a 5′ to 3′ DNA helicase that promotes replication fork progression through telomeric and subtelomeric DNA publication-title: Genes Dev. – volume: 103 start-page: 18196 year: 2006 end-page: 18201 ident: bib25 article-title: Suppression of spontaneous genome rearrangements in yeast DNA helicase mutants publication-title: Proc. Natl. Acad. Sci. USA – volume: 5 start-page: 739 year: 2004 end-page: 751 ident: bib1 article-title: The SCF ubiquitin ligase: Insights into a molecular machine publication-title: Nat. Rev. Mol. Cell Biol. – volume: 449 start-page: 356 year: 2007 end-page: 360 ident: bib29 article-title: ZEITLUPE is a circadian photoreceptor stabilized by GIGANTEA in blue light publication-title: Nature – volume: 19 start-page: 691 year: 2005 end-page: 697 ident: bib9 article-title: Mrc1 is required for normal progression of replication forks throughout chromatin in S. cerevisiae publication-title: Mol. Cell – volume: 279 start-page: 6674 year: 2004 end-page: 6682 ident: bib27 article-title: The amino-terminal portion of the F-box protein Met30p mediates its nuclear import and assimilation into an SCF complex publication-title: J. Biol. Chem. – volume: 124 start-page: 1069 year: 2006 end-page: 1081 ident: bib5 article-title: A DNA integrity network in the yeast Saccharomyces cerevisiae publication-title: Cell – volume: 15 start-page: 1736 year: 2004 end-page: 1745 ident: bib11 article-title: Identification of protein complexes required for efficient sister chromatid cohesion publication-title: Mol. Biol. Cell – volume: 19 start-page: 699 year: 2005 end-page: 706 ident: bib10 article-title: Mrc1 and Tof1 promote replication fork progression and recovery independently of Rad53 publication-title: Mol. Cell – volume: 21 start-page: 4938 year: 2001 end-page: 4948 ident: bib23 article-title: DNA replication forks pause at silent origins near the HML locus in budding yeast publication-title: Mol. Cell. Biol. – volume: 12 start-page: 1525 year: 2003 end-page: 1536 ident: bib24 article-title: The Saccharomyces cerevisiae helicase Rrm3p facilitates replication past nonhistone protein-DNA complexes publication-title: Mol. Cell – volume: 423 start-page: 720 year: 2003 end-page: 724 ident: bib31 article-title: Functional proteomic identification of DNA replication proteins by induced proteolysis in vivo publication-title: Nature – volume: 19 start-page: 691 year: 2005 ident: 10.1016/j.cub.2009.09.062_bib9 article-title: Mrc1 is required for normal progression of replication forks throughout chromatin in S. cerevisiae publication-title: Mol. Cell doi: 10.1016/j.molcel.2005.06.037 – volume: 347 start-page: 509 year: 2005 ident: 10.1016/j.cub.2009.09.062_bib12 article-title: Uncoupling of unwinding from DNA synthesis implies regulation of MCM helicase by Tof1/Mrc1/Csm3 checkpoint complex publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2005.01.041 – volume: 24 start-page: 4019 year: 2004 ident: 10.1016/j.cub.2009.09.062_bib22 article-title: Anatomy and dynamics of DNA replication fork movement in yeast telomeric regions publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.24.9.4019-4031.2004 – volume: 318 start-page: 261 year: 2007 ident: 10.1016/j.cub.2009.09.062_bib30 article-title: FKF1 and GIGANTEA complex formation is required for day-length measurement in Arabidopsis publication-title: Science doi: 10.1126/science.1146994 – volume: 32 start-page: 106 year: 2008 ident: 10.1016/j.cub.2009.09.062_bib16 article-title: Mrc1 and DNA polymerase ɛ function together in linking DNA replication and the S phase checkpoint publication-title: Mol. Cell doi: 10.1016/j.molcel.2008.08.020 – volume: 103 start-page: 897 year: 2006 ident: 10.1016/j.cub.2009.09.062_bib8 article-title: The Tof1p-Csm3p protein complex counteracts the Rrm3p helicase to control replication termination of Saccharomyces cerevisiae publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.0506540103 – volume: 423 start-page: 720 year: 2003 ident: 10.1016/j.cub.2009.09.062_bib31 article-title: Functional proteomic identification of DNA replication proteins by induced proteolysis in vivo publication-title: Nature doi: 10.1038/nature01692 – volume: 424 start-page: 1078 year: 2003 ident: 10.1016/j.cub.2009.09.062_bib13 article-title: S-phase checkpoint proteins Tof1 and Mrc1 form a stable replication-pausing complex publication-title: Nature doi: 10.1038/nature01900 – volume: 37 start-page: 495 year: 2009 ident: 10.1016/j.cub.2009.09.062_bib19 article-title: Control of genome stability by SLX protein complexes publication-title: Biochem. Soc. Trans. doi: 10.1042/BST0370495 – volume: 15 start-page: 1736 year: 2004 ident: 10.1016/j.cub.2009.09.062_bib11 article-title: Identification of protein complexes required for efficient sister chromatid cohesion publication-title: Mol. Biol. Cell doi: 10.1091/mbc.E03-08-0619 – volume: 19 start-page: 699 year: 2005 ident: 10.1016/j.cub.2009.09.062_bib10 article-title: Mrc1 and Tof1 promote replication fork progression and recovery independently of Rad53 publication-title: Mol. Cell doi: 10.1016/j.molcel.2005.07.028 – volume: 129 start-page: 1165 year: 2007 ident: 10.1016/j.cub.2009.09.062_bib28 article-title: Suprafacial orientation of the SCFCdc4 dimer accommodates multiple geometries for substrate ubiquitination publication-title: Cell doi: 10.1016/j.cell.2007.04.042 – volume: 103 start-page: 18196 year: 2006 ident: 10.1016/j.cub.2009.09.062_bib25 article-title: Suppression of spontaneous genome rearrangements in yeast DNA helicase mutants publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.0608566103 – volume: 28 start-page: 2992 year: 2009 ident: 10.1016/j.cub.2009.09.062_bib15 article-title: A key role for Ctf4 in coupling the MCM2-7 helicase to DNA polymerase alpha within the eukaryotic replisome publication-title: EMBO J. doi: 10.1038/emboj.2009.226 – volume: 279 start-page: 6674 year: 2004 ident: 10.1016/j.cub.2009.09.062_bib27 article-title: The amino-terminal portion of the F-box protein Met30p mediates its nuclear import and assimilation into an SCF complex publication-title: J. Biol. Chem. doi: 10.1074/jbc.M308875200 – volume: 17 start-page: 1540 year: 2006 ident: 10.1016/j.cub.2009.09.062_bib4 article-title: The F-box protein Dia2 regulates DNA replication publication-title: Mol. Biol. Cell doi: 10.1091/mbc.E05-09-0884 – volume: 34 start-page: 264 year: 2009 ident: 10.1016/j.cub.2009.09.062_bib18 article-title: Nucleases and helicases take center stage in homologous recombination publication-title: Trends Biochem. Sci. doi: 10.1016/j.tibs.2009.01.010 – volume: 174 start-page: 1709 year: 2006 ident: 10.1016/j.cub.2009.09.062_bib3 article-title: The F-box protein Dia2 overcomes replication impedance to promote genome stability in Saccharomyces cerevisiae publication-title: Genetics doi: 10.1534/genetics.106.057836 – volume: 8 start-page: 358 year: 2006 ident: 10.1016/j.cub.2009.09.062_bib6 article-title: GINS maintains association of Cdc45 with MCM in replisome progression complexes at eukaryotic DNA replication forks publication-title: Nat. Cell Biol. doi: 10.1038/ncb1382 – volume: 12 start-page: 1525 year: 2003 ident: 10.1016/j.cub.2009.09.062_bib24 article-title: The Saccharomyces cerevisiae helicase Rrm3p facilitates replication past nonhistone protein-DNA complexes publication-title: Mol. Cell doi: 10.1016/S1097-2765(03)00456-8 – volume: 176 start-page: 1417 year: 2007 ident: 10.1016/j.cub.2009.09.062_bib14 article-title: Genetic dissection of parallel sister-chromatid cohesion pathways publication-title: Genetics doi: 10.1534/genetics.107.072876 – volume: 16 start-page: 1383 year: 2002 ident: 10.1016/j.cub.2009.09.062_bib21 article-title: Saccharomyces Rrm3p, a 5′ to 3′ DNA helicase that promotes replication fork progression through telomeric and subtelomeric DNA publication-title: Genes Dev. doi: 10.1101/gad.982902 – volume: 16 start-page: 5966 year: 1997 ident: 10.1016/j.cub.2009.09.062_bib17 article-title: The Cdc4/34/53 pathway targets Cdc6p for proteolysis in budding yeast publication-title: EMBO J. doi: 10.1093/emboj/16.19.5966 – volume: 449 start-page: 356 year: 2007 ident: 10.1016/j.cub.2009.09.062_bib29 article-title: ZEITLUPE is a circadian photoreceptor stabilized by GIGANTEA in blue light publication-title: Nature doi: 10.1038/nature06132 – volume: 21 start-page: 4938 year: 2001 ident: 10.1016/j.cub.2009.09.062_bib23 article-title: DNA replication forks pause at silent origins near the HML locus in budding yeast publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.21.15.4938-4948.2001 – volume: 5 start-page: 739 year: 2004 ident: 10.1016/j.cub.2009.09.062_bib1 article-title: The SCF ubiquitin ligase: Insights into a molecular machine publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm1471 – volume: 1695 start-page: 133 year: 2004 ident: 10.1016/j.cub.2009.09.062_bib2 article-title: A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbamcr.2004.09.027 – volume: 19 start-page: 1905 year: 2005 ident: 10.1016/j.cub.2009.09.062_bib7 article-title: Molecular anatomy and regulation of a stable replisome at a paused eukaryotic DNA replication fork publication-title: Genes Dev. doi: 10.1101/gad.337205 – volume: 3 start-page: e228 year: 2007 ident: 10.1016/j.cub.2009.09.062_bib26 article-title: Genome-wide analysis of Rad52 foci reveals diverse mechanisms impacting recombination publication-title: PLoS Genet. doi: 10.1371/journal.pgen.0030228 – volume: 124 start-page: 1069 year: 2006 ident: 10.1016/j.cub.2009.09.062_bib5 article-title: A DNA integrity network in the yeast Saccharomyces cerevisiae publication-title: Cell doi: 10.1016/j.cell.2005.12.036 – volume: 12 start-page: 4056 year: 1992 ident: 10.1016/j.cub.2009.09.062_bib20 article-title: Replication forks pause at yeast centromeres publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.12.9.4056 |
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Snippet | Eukaryotic cells contain multiple versions of the E3 ubiquitin ligase known as the SCF (Skp1/cullin/F box), each of which is distinguished by a different F box... |
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SubjectTerms | DNA |
Title | The Amino-Terminal TPR Domain of Dia2 Tethers SCFDia2 to the Replisome Progression Complex |
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