The High-mobility-group Box Protein SSRP1/T160 is Essential for Cell Viability in Day 3.5 Mouse Embryos

Overview

Journal Mol Cell Biol

Specialty Cell Biology

Date 2003 Jul 16

PMID 12861016

Citations 41

Authors

Shang Cao

Heather Bendall

Geoffrey G Hicks

Abudi Nashabi

Hitoshi Sakano

Yoichi Shinkai

Marisa Gariglio

Eugene M Oltz

H Earl Ruley

Affiliations

Soon will be listed here.

Abstract

The high-mobility-group (HMG) SSRP1 protein is a member of a conserved chromatin-remodeling complex (FACT/DUF/CP) implicated in DNA replication, basal and regulated transcription, and DNA repair. To assist in the functional analysis of SSRP1, the Ssrp1 gene was targeted in murine embryonic stem cells, and the mutation was introduced into the germ line. Embryos homozygous for the targeted allele die soon after implantation, and preimplantation blastocysts are defective for cell outgrowth and/or survival in vitro. The Ssrp1 mutation was also crossed into a p53 null background without affecting growth and/or survival defects caused by loss of Ssrp1 function. Thus, Ssrp1 appears to encode nonredundant and p53-independent functions that are essential for cell viability.

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References

Brewster N, Johnston G, Singer R . A bipartite yeast SSRP1 analog comprised of Pob3 and Nhp6 proteins modulates transcription. Mol Cell Biol. 2001; 21(10):3491-502. PMC: 100271. DOI: 10.1128/MCB.21.10.3491-3502.2001. View

Prendergast J, Murray L, Rowley A, Carruthers D, Singer R, Johnston G . Size selection identifies new genes that regulate Saccharomyces cerevisiae cell proliferation. Genetics. 1990; 124(1):81-90. PMC: 1203912. DOI: 10.1093/genetics/124.1.81. View

Keller D, Zeng X, Wang Y, Zhang Q, Kapoor M, Shu H . A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1. Mol Cell. 2001; 7(2):283-92. DOI: 10.1016/s1097-2765(01)00176-9. View

Lowe S, Schmitt E, Smith S, Osborne B, Jacks T . p53 is required for radiation-induced apoptosis in mouse thymocytes. Nature. 1993; 362(6423):847-9. DOI: 10.1038/362847a0. View

Formosa T, Eriksson P, Wittmeyer J, Ginn J, Yu Y, Stillman D . Spt16-Pob3 and the HMG protein Nhp6 combine to form the nucleosome-binding factor SPN. EMBO J. 2001; 20(13):3506-17. PMC: 125512. DOI: 10.1093/emboj/20.13.3506. View

Wittmeyer J, Formosa T . The Saccharomyces cerevisiae DNA polymerase alpha catalytic subunit interacts with Cdc68/Spt16 and with Pob3, a protein similar to an HMG1-like protein. Mol Cell Biol. 1997; 17(7):4178-90. PMC: 232271. DOI: 10.1128/MCB.17.7.4178. View

Bustin M . Regulation of DNA-dependent activities by the functional motifs of the high-mobility-group chromosomal proteins. Mol Cell Biol. 1999; 19(8):5237-46. PMC: 84367. DOI: 10.1128/MCB.19.8.5237. View

Kelley D, Stokes D, PERRY R . CHD1 interacts with SSRP1 and depends on both its chromodomain and its ATPase/helicase-like domain for proper association with chromatin. Chromosoma. 1999; 108(1):10-25. DOI: 10.1007/s004120050347. View

Hertel L, De Andrea M, Bellomo G, Santoro P, Landolfo S, Gariglio M . The HMG protein T160 colocalizes with DNA replication foci and is down-regulated during cell differentiation. Exp Cell Res. 1999; 250(2):313-28. DOI: 10.1006/excr.1999.4495. View

10.

Calogero S, Grassi F, Aguzzi A, Voigtlander T, Ferrier P, Ferrari S . The lack of chromosomal protein Hmg1 does not disrupt cell growth but causes lethal hypoglycaemia in newborn mice. Nat Genet. 1999; 22(3):276-80. DOI: 10.1038/10338. View

11.

Shirakata M, Huppi K, Usuda S, Okazaki K, Yoshida K, Sakano H . HMG1-related DNA-binding protein isolated with V-(D)-J recombination signal probes. Mol Cell Biol. 1991; 11(9):4528-36. PMC: 361327. DOI: 10.1128/mcb.11.9.4528-4536.1991. View

12.

Brewster N, Johnston G, Singer R . Characterization of the CP complex, an abundant dimer of Cdc68 and Pob3 proteins that regulates yeast transcriptional activation and chromatin repression. J Biol Chem. 1998; 273(34):21972-9. DOI: 10.1074/jbc.273.34.21972. View

13.

Frank K, Sharpless N, Gao Y, Sekiguchi J, Ferguson D, Zhu C . DNA ligase IV deficiency in mice leads to defective neurogenesis and embryonic lethality via the p53 pathway. Mol Cell. 2000; 5(6):993-1002. DOI: 10.1016/s1097-2765(00)80264-6. View

14.

Nagulapalli S, Pongubala J, Atchison M . Multiple proteins physically interact with PU.1. Transcriptional synergy with NF-IL6 beta (C/EBP delta, CRP3). J Immunol. 1995; 155(9):4330-8. View

15.

Staal F, Clevers H . Tcf/Lef transcription factors during T-cell development: unique and overlapping functions. Hematol J. 2002; 1(1):3-6. DOI: 10.1038/sj.thj.6200001. View

16.

Zeng S, Dai M, Keller D, Lu H . SSRP1 functions as a co-activator of the transcriptional activator p63. EMBO J. 2002; 21(20):5487-97. PMC: 129072. DOI: 10.1093/emboj/cdf540. View

17.

Malone E, Clark C, Chiang A, Winston F . Mutations in SPT16/CDC68 suppress cis- and trans-acting mutations that affect promoter function in Saccharomyces cerevisiae. Mol Cell Biol. 1991; 11(11):5710-7. PMC: 361942. DOI: 10.1128/mcb.11.11.5710-5717.1991. View

18.

Bruhn S, Pil P, Essigmann J, Housman D, Lippard S . Isolation and characterization of human cDNA clones encoding a high mobility group box protein that recognizes structural distortions to DNA caused by binding of the anticancer agent cisplatin. Proc Natl Acad Sci U S A. 1992; 89(6):2307-11. PMC: 48646. DOI: 10.1073/pnas.89.6.2307. View

19.

Kanai-Azuma M, Kanai Y, Gad J, Tajima Y, Taya C, Kurohmaru M . Depletion of definitive gut endoderm in Sox17-null mutant mice. Development. 2002; 129(10):2367-79. DOI: 10.1242/dev.129.10.2367. View

20.

Krogan N, Kim M, Ahn S, Zhong G, Kobor M, Cagney G . RNA polymerase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approach. Mol Cell Biol. 2002; 22(20):6979-92. PMC: 139818. DOI: 10.1128/MCB.22.20.6979-6992.2002. View