Human major HSP70 protein complements the localization and functional defects of cytoplasmic mutant SV40 T antigen in Swiss 3T3 mouse fibroblast cells - PubMed (original) (raw)

. 1991 Dec;5(12A):2235-44.

doi: 10.1101/gad.5.12a.2235.

Affiliations

• PMID: 1748281
• DOI: 10.1101/gad.5.12a.2235

Free article

Human major HSP70 protein complements the localization and functional defects of cytoplasmic mutant SV40 T antigen in Swiss 3T3 mouse fibroblast cells

D I Jeoung et al. Genes Dev. 1991 Dec.

Free article

Abstract

The CT3 cytoplasmic localization mutant of SV40 T antigen is neither properly transported to the nucleus nor is it functional in rodent cells. Human precrisis cells are able to complement this mutation, as they are fully transformed by CT3 with wild-type efficiency. The human-specific factors responsible for this species-specific difference in response to CT3 were localized to human chromosome 6 by synteny in a panel of six somatic cell hybrids. A major human HSP70 heat shock protein located on chromosome 6 is expressed constitutively in human cells. Hsp70 proteins have been reported to play a role in intracellular movement of newly synthesized proteins. To test whether human HSP70 played a role in the complementation by human cells of the defect of CT3, we constructed a series of mouse cell lines expressing human HSP70 and tested them for their ability to localize CT3 T antigen in the nucleus and for their ability to be transformed by CT3 DNA. Mouse cell lines expressing human HSP70 protein were able to translocate mutant CT3 T antigen into the nucleus and were transformed by CT3 at rates comparable with wild-type SV40. Mouse-inducible HSP70 protein was not able to translocate cytoplasmic T antigen in Swiss 3T3 mouse fibroblast cells, even after heat shock. Apparently human HSP70 is capable of complementing directly or indirectly the structural and functional alterations in SV40 T antigen introduced by the CT3 mutation.

PubMed Disclaimer

Similar articles

• Transformation of precrisis human cells by the simian virus 40 cytoplasmic-localization mutant pSVCT3 is accompanied by nuclear T antigen.
  Chen S, Levesque P, Pomert E, Pollack RE. Chen S, et al. J Virol. 1987 Nov;61(11):3521-7. doi: 10.1128/JVI.61.11.3521-3527.1987. J Virol. 1987. PMID: 2822959 Free PMC article.
• Effect on polyomavirus T-antigen function of mutations in a conserved leucine-rich segment of the DnaJ domain.
  Li H, Söderbärg K, Houshmand H, You ZY, Magnusson G. Li H, et al. J Virol. 2001 Mar;75(5):2253-61. doi: 10.1128/JVI.75.5.2253-2261.2001. J Virol. 2001. PMID: 11160729 Free PMC article.
• An SV40 transformation revertant due to a host mutation: isolation and complementation analysis.
  Silverstein GH, Kohrman DC, Christensen JB, Brockman WW, Imperiale MJ. Silverstein GH, et al. Virology. 1992 Apr;187(2):723-33. doi: 10.1016/0042-6822(92)90475-5. Virology. 1992. PMID: 1312274
• Immunological evidence for the association between simian virus 40 115-kDa super T antigen and hsp70 proteins in rat, monkey, and human cells.
  May E, Breugnot C, Duthu A, May P. May E, et al. Virology. 1991 Jan;180(1):285-93. doi: 10.1016/0042-6822(91)90033-8. Virology. 1991. PMID: 1701947
• Construction of SV40 deletion mutants and delimitation of the binding domain for heat shock protein to the amino terminus of large T-antigen.
  Sawai ET, Rasmussen G, Butel JS. Sawai ET, et al. Virus Res. 1994 Mar;31(3):367-78. doi: 10.1016/0168-1702(94)90029-9. Virus Res. 1994. PMID: 8191789

Cited by

• HIV-1 viral protein R (Vpr) and its interactions with host cell.
  Li G, Bukrinsky M, Zhao RY. Li G, et al. Curr HIV Res. 2009 Mar;7(2):178-83. doi: 10.2174/157016209787581436. Curr HIV Res. 2009. PMID: 19275587 Free PMC article. Review.
• Overexpression of heat shock protein 70 restores the structural stability and functional defects of temperature-sensitive mutant of large T antigen at nonpermissive temperature.
  Tabuchi Y, Kuribayashi R, Takasaki I, Doi T, Sakai H, Takeguchi N, Kondo T, Ohtsuka K. Tabuchi Y, et al. Cell Stress Chaperones. 2006 Autumn;11(3):259-67. doi: 10.1379/csc-193r.1. Cell Stress Chaperones. 2006. PMID: 17009599 Free PMC article.
• Paeoniflorin, a novel heat shock protein-inducing compound.
  Yan D, Saito K, Ohmi Y, Fujie N, Ohtsuka K. Yan D, et al. Cell Stress Chaperones. 2004 Winter;9(4):378-89. doi: 10.1379/csc-51r.1. Cell Stress Chaperones. 2004. PMID: 15633296 Free PMC article.
• Heat shock protein 90 and the nuclear transport of progesterone receptor.
  Haverinen M, Passinen S, Syvälä H, Pasanen S, Manninen T, Tuohimaa P, Ylikomi T. Haverinen M, et al. Cell Stress Chaperones. 2001 Jul;6(3):256-62. doi: 10.1379/1466-1268(2001)006<0256:hspatn>2.0.co;2. Cell Stress Chaperones. 2001. PMID: 11599567 Free PMC article.
• FANCC interacts with Hsp70 to protect hematopoietic cells from IFN-gamma/TNF-alpha-mediated cytotoxicity.
  Pang Q, Keeble W, Christianson TA, Faulkner GR, Bagby GC. Pang Q, et al. EMBO J. 2001 Aug 15;20(16):4478-89. doi: 10.1093/emboj/20.16.4478. EMBO J. 2001. PMID: 11500375 Free PMC article.

Publication types

MeSH terms

Substances

LinkOut - more resources

• Full Text Sources

  • HighWire