22
Xenopus
Furstenthal, L., Kaiser, B.K., Swanson, C., Jackson, P.K., 2001a.
Cyclin E uses Cdc6 as a chromatin-associated receptor
required for DNA replication. J Cell Biology 152, 1267–
1278. https://doi.org/10.1083/jcb.152.6.1267
Furstenthal, L., Swanson, C., Kaiser, B.K., Eldridge, A.G., Jackson,
P.K., 2001b. Triggering ubiquitination of a CDK inhibitor at
origins of DNA replication. Nat Cell Biol 3, 715–722. https://
doi.org/10.1038/35087026
Gabrielli, B.G., Lee, M.S., Walker, D.H., Piwnica-Worms, H.,
Maller, J.L., 1992. Cdc25 regulates the phosphorylation
and activity of the Xenopus cdk2 protein kinase complex.
J Biol Chem 267, 18040–18046. https://doi.org/10.1016/
s0021-9258(19)37149-2
Garner, E., Costanzo, V., 2009. Studying the DNA damage response
using in vitro model systems. Dna Repair 8, 1025–1037.
https://doi.org/10.1016/j.dnarep.2009.04.015
Gautier, J., Solomon, M.J., Booher, R.N., Bazan, J.F., Kirschner,
M.W., 1991. Cdc25 is a specifc tyrosine phosphatase that
directly activates p34cdc2. Cell 67, 197–211. https://doi.
org/10.1016/0092-8674(91)90583-k
Gerhart, J., Wu, M., Kirschner, M., 1984. Cell cycle dynamics of
an M-phase-specifc cytoplasmic factor in Xenopus laevis
oocytes and eggs. J Cell Biology 98, 1247–1255. https://doi.
org/10.1083/jcb.98.4.1247
Glotzer, M., Murray, A., Kirschner, M., 1991. Cyclin is degraded
by the ubiquitin pathway. Nature 349, 132–138.
Graham, C.F., Arms, K., Gurdon, J.B., 1966. The induction of DNA
synthesis by frog egg cytoplasm. Dev Biol 14, 349–381.
https://doi.org/10.1016/0012-1606(66)90020-0
Gruszka, D.T., Xie, S., Kimura, H., Yardimci, H., 2020. Singlemolecule imaging reveals control of parental histone recycling by free histones during DNA replication. Sci Adv 6,
eabc0330. https://doi.org/10.1126/sciadv.abc0330
Gurdon, J.B., 1962. Adult frogs derived from the nuclei of single
somatic cells. Developmental Biology 4, 256–273.
Hara, K., Tydeman, P., Kirschner, M., 1980. A cytoplasmic
clock with the same period as the division cycle in Xenopus
eggs. Proc National Acad Sci 77, 462–466. https://doi.org/
10.1073/pnas.77.1.462
Harland, R.M., Laskey, R.A., 1980. Regulated replication of DNA
microinjected into eggs of Xenopus laevis. Cell 21, 761–771.
https://doi.org/10.1016/0092-8674(80)90439-0
Hartwell, L.H., Culotti, J., Pringle, J.R., Reid, B.J., 1974. Genetic
control of the cell division cycle in yeast. Science 183, 46–51.
https://doi.org/10.1126/science.183.4120.46
Havens, C.G., Walter, J.C., 2009. Docking of a specialized PIP Box
onto chromatin-bound PCNA creates a degron for the ubiquitin ligase CRL4Cdt2. Molecular Cell 35, 93–104. https://
doi.org/10.1016/j.molcel.2009.05.012
Herrick, J., Stanislawski, P., Hyrien, O., Bensimon, A., 2000.
Replication fork density increases during DNA synthesis in
X. laevis egg extracts. J Mol Biol 300, 1133–1142. https://
doi.org/10.1006/jmbi.2000.3930
Higashi, T.L., Ikeda, M., Tanaka, H., Nakagawa, T., Bando, M.,
Shirahige, K., Kubota, Y., Takisawa, H., Masukata, H.,
Takahashi, T.S., 2012. The prereplication complex recruits
XEco2 to chromatin to promote cohesin acetylation in
Xenopus egg extracts. Current Biology: CB 22, 977–988.
https://doi.org/10.1016/j.cub.2012.04.013
Hodskinson, M.R., Bolner, A., Sato, K., Kamimae-Lanning, A.N.,
Rooijers, K., Witte, M., Mahesh, M., Silhan, J., Petek, M.,
Williams, D.M., Kind, J., Chin, J.W., Patel, K.J., Knipscheer,
P., 2020. Alcohol-derived DNA crosslinks are repaired by
two distinct mechanisms. Nature 579, 603–608. https://doi.
org/10.1038/s41586-020-2059-5
Hoogenboom, W.S., Douwel, D.K., Knipscheer, P., 2017. Xenopus
egg extract: A powerful tool to study genome maintenance mechanisms. Dev Biol 428, 300–309. https://doi.
org/10.1016/j.ydbio.2017.03.033
Hwang, H.C., Clurman, B.E., 2005. Cyclin E in normal and neoplastic cell cycles. Oncogene 24, 2776–2786. https://doi.
org/10.1038/sj.onc.1208613
Irniger, S., Piatti, S., Michaelis, C., Nasmyth, K., 1995. Genes
involved in sister chromatid separation are needed for b-type
cyclin proteolysis in budding yeast. Cell 81, 269–277. https://
doi.org/10.1016/0092-8674(95)90337-2
Izumi, T., Walker, D.H., Maller, J.L., 1992. Periodic changes in
phosphorylation of the Xenopus cdc25 phosphatase regulate
its activity. Mol Biol Cell 3, 927–939. https://doi.org/10.1091/
mbc.3.8.927
Jares, P., Blow, J.J., 2000. Xenopus cdc7 function is dependent on
licensing but not on XORC, XCdc6, or CDK activity and
is required for XCdc45 loading. Genes & Development 14,
1528–1540.
Jares, P., Luciani, M.G., Blow, J.J., 2004. A Xenopus Dbf4 homolog
is required for Cdc7 chromatin binding and DNA replication.
Bmc Mol Biol 5, 5. https://doi.org/10.1186/1471-2199-5-5
Kanke, M., Tahara, E., Veld, P.J.H. in’t, Nishiyama, T., 2016.
Cohesin acetylation and Wapl-Pds5 oppositely regulate
translocation of cohesin along DNA. The EMBO Journal 35,
2686–2698. https://doi.org/10.15252/embj.201695756
Kim, S.Y., Ferrell, J.E., 2007. Substrate competition as a source of
ultrasensitivity in the inactivation of Wee1. Cell 128, 1133–
1145. https://doi.org/10.1016/j.cell.2007.01.039
King, R., Lustig, K., Stukenberg, P., McGarry, T., Kirschner, M., 1997.
Expression cloning in the test tube. Science 277, 973–974.
King, R., Peters, J., Tugendreich, S., Rolfe, M., Hieter, P.,
Kirschner, M., 1995. A 20S complex containing CDC27 and
CDC16 catalyzes the mitosis-specifc conjugation of ubiquitin to cyclin B. Cell 81, 279–288.
Kirschner, M., 2020. What makes the cell cycle tick? a celebration of the awesome power of biochemistry and the frog egg.
Mol Biol Cell 31, 2874–2878. https://doi.org/10.1091/mbc.
e20-10-0626
Kose, H.B., Larsen, N.B., Duxin, J.P., Yardimci, H., 2019.
Dynamics of the eukaryotic replicative helicase at laggingstrand protein barriers support the steric exclusion model.
Cell Reports 26, 2113–2125.e6. https://doi.org/10.1016/j.
celrep.2019.01.086
Kubota, Y., Mimura, S., Nishimoto, S., Masuda, T., Nojima, H.,
Takisawa, H., 1997. Licensing of DNA replication by a
multi-protein complex of MCM/P1 proteins in Xenopus
eggs. Embo J 16, 3320–3331. https://doi.org/10.1093/emboj/
16.11.3320
Kubota, Y., Mimura, S., Nishimoto, S., Takisawa, H., Nojima,
H., 1995. Identifcation of the yeast MCM3-related protein as a component of Xenopus DNA replication licensing factor. Cell 81, 601–609. https://doi.org/10.1016/
0092-8674(95)90081-0
Kubota, Y., Takase, Y., Komori, Y., Hashimoto, Y., Arata, T.,
Kamimura, Y., Araki, H., Takisawa, H., 2003. A novel ringlike complex of Xenopus proteins essential for the initiation
of DNA replication. Genes & Development 17, 1141–1152.
https://doi.org/10.1101/gad.1070003
Kumagai, A., Dunphy, W.G., 1991. The cdc25 protein controls
tyrosine dephosphorylation of the cdc2 protein in a cellfree system. Cell 64, 903–914. https://doi.org/10.1016/
0092-8674(91)90315-p
Kumagai, A., Dunphy, W.G., 2017. MTBP, the partner of treslin, contains a novel DNA-binding domain, that is essential for proper
Xenopus
Furstenthal, L., Kaiser, B.K., Swanson, C., Jackson, P.K., 2001a.
Cyclin E uses Cdc6 as a chromatin-associated receptor
required for DNA replication. J Cell Biology 152, 1267–
1278. https://doi.org/10.1083/jcb.152.6.1267
Furstenthal, L., Swanson, C., Kaiser, B.K., Eldridge, A.G., Jackson,
P.K., 2001b. Triggering ubiquitination of a CDK inhibitor at
origins of DNA replication. Nat Cell Biol 3, 715–722. https://
doi.org/10.1038/35087026
Gabrielli, B.G., Lee, M.S., Walker, D.H., Piwnica-Worms, H.,
Maller, J.L., 1992. Cdc25 regulates the phosphorylation
and activity of the Xenopus cdk2 protein kinase complex.
J Biol Chem 267, 18040–18046. https://doi.org/10.1016/
s0021-9258(19)37149-2
Garner, E., Costanzo, V., 2009. Studying the DNA damage response
using in vitro model systems. Dna Repair 8, 1025–1037.
https://doi.org/10.1016/j.dnarep.2009.04.015
Gautier, J., Solomon, M.J., Booher, R.N., Bazan, J.F., Kirschner,
M.W., 1991. Cdc25 is a specifc tyrosine phosphatase that
directly activates p34cdc2. Cell 67, 197–211. https://doi.
org/10.1016/0092-8674(91)90583-k
Gerhart, J., Wu, M., Kirschner, M., 1984. Cell cycle dynamics of
an M-phase-specifc cytoplasmic factor in Xenopus laevis
oocytes and eggs. J Cell Biology 98, 1247–1255. https://doi.
org/10.1083/jcb.98.4.1247
Glotzer, M., Murray, A., Kirschner, M., 1991. Cyclin is degraded
by the ubiquitin pathway. Nature 349, 132–138.
Graham, C.F., Arms, K., Gurdon, J.B., 1966. The induction of DNA
synthesis by frog egg cytoplasm. Dev Biol 14, 349–381.
https://doi.org/10.1016/0012-1606(66)90020-0
Gruszka, D.T., Xie, S., Kimura, H., Yardimci, H., 2020. Singlemolecule imaging reveals control of parental histone recycling by free histones during DNA replication. Sci Adv 6,
eabc0330. https://doi.org/10.1126/sciadv.abc0330
Gurdon, J.B., 1962. Adult frogs derived from the nuclei of single
somatic cells. Developmental Biology 4, 256–273.
Hara, K., Tydeman, P., Kirschner, M., 1980. A cytoplasmic
clock with the same period as the division cycle in Xenopus
eggs. Proc National Acad Sci 77, 462–466. https://doi.org/
10.1073/pnas.77.1.462
Harland, R.M., Laskey, R.A., 1980. Regulated replication of DNA
microinjected into eggs of Xenopus laevis. Cell 21, 761–771.
https://doi.org/10.1016/0092-8674(80)90439-0
Hartwell, L.H., Culotti, J., Pringle, J.R., Reid, B.J., 1974. Genetic
control of the cell division cycle in yeast. Science 183, 46–51.
https://doi.org/10.1126/science.183.4120.46
Havens, C.G., Walter, J.C., 2009. Docking of a specialized PIP Box
onto chromatin-bound PCNA creates a degron for the ubiquitin ligase CRL4Cdt2. Molecular Cell 35, 93–104. https://
doi.org/10.1016/j.molcel.2009.05.012
Herrick, J., Stanislawski, P., Hyrien, O., Bensimon, A., 2000.
Replication fork density increases during DNA synthesis in
X. laevis egg extracts. J Mol Biol 300, 1133–1142. https://
doi.org/10.1006/jmbi.2000.3930
Higashi, T.L., Ikeda, M., Tanaka, H., Nakagawa, T., Bando, M.,
Shirahige, K., Kubota, Y., Takisawa, H., Masukata, H.,
Takahashi, T.S., 2012. The prereplication complex recruits
XEco2 to chromatin to promote cohesin acetylation in
Xenopus egg extracts. Current Biology: CB 22, 977–988.
https://doi.org/10.1016/j.cub.2012.04.013
Hodskinson, M.R., Bolner, A., Sato, K., Kamimae-Lanning, A.N.,
Rooijers, K., Witte, M., Mahesh, M., Silhan, J., Petek, M.,
Williams, D.M., Kind, J., Chin, J.W., Patel, K.J., Knipscheer,
P., 2020. Alcohol-derived DNA crosslinks are repaired by
two distinct mechanisms. Nature 579, 603–608. https://doi.
org/10.1038/s41586-020-2059-5
Hoogenboom, W.S., Douwel, D.K., Knipscheer, P., 2017. Xenopus
egg extract: A powerful tool to study genome maintenance mechanisms. Dev Biol 428, 300–309. https://doi.
org/10.1016/j.ydbio.2017.03.033
Hwang, H.C., Clurman, B.E., 2005. Cyclin E in normal and neoplastic cell cycles. Oncogene 24, 2776–2786. https://doi.
org/10.1038/sj.onc.1208613
Irniger, S., Piatti, S., Michaelis, C., Nasmyth, K., 1995. Genes
involved in sister chromatid separation are needed for b-type
cyclin proteolysis in budding yeast. Cell 81, 269–277. https://
doi.org/10.1016/0092-8674(95)90337-2
Izumi, T., Walker, D.H., Maller, J.L., 1992. Periodic changes in
phosphorylation of the Xenopus cdc25 phosphatase regulate
its activity. Mol Biol Cell 3, 927–939. https://doi.org/10.1091/
mbc.3.8.927
Jares, P., Blow, J.J., 2000. Xenopus cdc7 function is dependent on
licensing but not on XORC, XCdc6, or CDK activity and
is required for XCdc45 loading. Genes & Development 14,
1528–1540.
Jares, P., Luciani, M.G., Blow, J.J., 2004. A Xenopus Dbf4 homolog
is required for Cdc7 chromatin binding and DNA replication.
Bmc Mol Biol 5, 5. https://doi.org/10.1186/1471-2199-5-5
Kanke, M., Tahara, E., Veld, P.J.H. in’t, Nishiyama, T., 2016.
Cohesin acetylation and Wapl-Pds5 oppositely regulate
translocation of cohesin along DNA. The EMBO Journal 35,
2686–2698. https://doi.org/10.15252/embj.201695756
Kim, S.Y., Ferrell, J.E., 2007. Substrate competition as a source of
ultrasensitivity in the inactivation of Wee1. Cell 128, 1133–
1145. https://doi.org/10.1016/j.cell.2007.01.039
King, R., Lustig, K., Stukenberg, P., McGarry, T., Kirschner, M., 1997.
Expression cloning in the test tube. Science 277, 973–974.
King, R., Peters, J., Tugendreich, S., Rolfe, M., Hieter, P.,
Kirschner, M., 1995. A 20S complex containing CDC27 and
CDC16 catalyzes the mitosis-specifc conjugation of ubiquitin to cyclin B. Cell 81, 279–288.
Kirschner, M., 2020. What makes the cell cycle tick? a celebration of the awesome power of biochemistry and the frog egg.
Mol Biol Cell 31, 2874–2878. https://doi.org/10.1091/mbc.
e20-10-0626
Kose, H.B., Larsen, N.B., Duxin, J.P., Yardimci, H., 2019.
Dynamics of the eukaryotic replicative helicase at laggingstrand protein barriers support the steric exclusion model.
Cell Reports 26, 2113–2125.e6. https://doi.org/10.1016/j.
celrep.2019.01.086
Kubota, Y., Mimura, S., Nishimoto, S., Masuda, T., Nojima, H.,
Takisawa, H., 1997. Licensing of DNA replication by a
multi-protein complex of MCM/P1 proteins in Xenopus
eggs. Embo J 16, 3320–3331. https://doi.org/10.1093/emboj/
16.11.3320
Kubota, Y., Mimura, S., Nishimoto, S., Takisawa, H., Nojima,
H., 1995. Identifcation of the yeast MCM3-related protein as a component of Xenopus DNA replication licensing factor. Cell 81, 601–609. https://doi.org/10.1016/
0092-8674(95)90081-0
Kubota, Y., Takase, Y., Komori, Y., Hashimoto, Y., Arata, T.,
Kamimura, Y., Araki, H., Takisawa, H., 2003. A novel ringlike complex of Xenopus proteins essential for the initiation
of DNA replication. Genes & Development 17, 1141–1152.
https://doi.org/10.1101/gad.1070003
Kumagai, A., Dunphy, W.G., 1991. The cdc25 protein controls
tyrosine dephosphorylation of the cdc2 protein in a cellfree system. Cell 64, 903–914. https://doi.org/10.1016/
0092-8674(91)90315-p
Kumagai, A., Dunphy, W.G., 2017. MTBP, the partner of treslin, contains a novel DNA-binding domain, that is essential for proper