Simian virus 40 large T antigen binds a novel Bcl-2 homology domain 3- containing proapoptosis protein in the cytoplasm

Shih Chong Tsai, Kishore B S Pasumarthi, Laura Pajak, Michael Franklin, Brian Patton, He Wang, William J. Henzel, John T. Stults, Loren Field

Research output: Contribution to journalArticle

59 Citations (Scopus)

Abstract

A 193-kDa SV40 large T antigen (T-Ag)-binding protein, designated p193, was identified and cloned. Inspection of the deduced amino acid sequence revealed the presence of a short motif similar to the Bcl-2 homology (BH) domain 3, suggesting that p193 may be a member of a family of apoptosis promoting proteins containing only BH3 motifs. In support of this, p193 expression promoted apoptosis in NIH-3T3 cells. Deletion of the BH3 motif abolished p193 apoptosis activity, p193-induced apoptosis was antagonized by co-expression of Bcl-X(L). Immune cytologic analysis indicated that p193 is localized to the cytoplasm of transfected cells, p193-induced apoptosis was also antagonized by co-expression of T-Ag, which resulted in the cytoplasmic localization of both proteins. The p193 binding site was mapped to an N- terminal region of T-Ag previously implicated in transforming activity. These results suggest that T-Ag possesses an antiapoptosis activity, independent of p53 sequestration, which is actuated by T-Ag/p193 binding in the cytoplasm.

Original languageEnglish
Pages (from-to)3239-3246
Number of pages8
JournalJournal of Biological Chemistry
Volume275
Issue number5
DOIs
StatePublished - Feb 4 2000

Fingerprint

Simian virus 40
Viral Tumor Antigens
Viruses
Cytoplasm
Apoptosis
Proteins
Polyomavirus Transforming Antigens
NIH 3T3 Cells
Amino Acid Sequence
Carrier Proteins
Inspection
Binding Sites
Amino Acids

ASJC Scopus subject areas

  • Biochemistry

Cite this

Simian virus 40 large T antigen binds a novel Bcl-2 homology domain 3- containing proapoptosis protein in the cytoplasm. / Tsai, Shih Chong; Pasumarthi, Kishore B S; Pajak, Laura; Franklin, Michael; Patton, Brian; Wang, He; Henzel, William J.; Stults, John T.; Field, Loren.

In: Journal of Biological Chemistry, Vol. 275, No. 5, 04.02.2000, p. 3239-3246.

Research output: Contribution to journalArticle

Tsai, SC, Pasumarthi, KBS, Pajak, L, Franklin, M, Patton, B, Wang, H, Henzel, WJ, Stults, JT & Field, L 2000, 'Simian virus 40 large T antigen binds a novel Bcl-2 homology domain 3- containing proapoptosis protein in the cytoplasm', Journal of Biological Chemistry, vol. 275, no. 5, pp. 3239-3246. https://doi.org/10.1074/jbc.275.5.3239
Tsai, Shih Chong ; Pasumarthi, Kishore B S ; Pajak, Laura ; Franklin, Michael ; Patton, Brian ; Wang, He ; Henzel, William J. ; Stults, John T. ; Field, Loren. / Simian virus 40 large T antigen binds a novel Bcl-2 homology domain 3- containing proapoptosis protein in the cytoplasm. In: Journal of Biological Chemistry. 2000 ; Vol. 275, No. 5. pp. 3239-3246.
@article{1c1d137abc8e4e21a9a12de2b96d6000,
title = "Simian virus 40 large T antigen binds a novel Bcl-2 homology domain 3- containing proapoptosis protein in the cytoplasm",
abstract = "A 193-kDa SV40 large T antigen (T-Ag)-binding protein, designated p193, was identified and cloned. Inspection of the deduced amino acid sequence revealed the presence of a short motif similar to the Bcl-2 homology (BH) domain 3, suggesting that p193 may be a member of a family of apoptosis promoting proteins containing only BH3 motifs. In support of this, p193 expression promoted apoptosis in NIH-3T3 cells. Deletion of the BH3 motif abolished p193 apoptosis activity, p193-induced apoptosis was antagonized by co-expression of Bcl-X(L). Immune cytologic analysis indicated that p193 is localized to the cytoplasm of transfected cells, p193-induced apoptosis was also antagonized by co-expression of T-Ag, which resulted in the cytoplasmic localization of both proteins. The p193 binding site was mapped to an N- terminal region of T-Ag previously implicated in transforming activity. These results suggest that T-Ag possesses an antiapoptosis activity, independent of p53 sequestration, which is actuated by T-Ag/p193 binding in the cytoplasm.",
author = "Tsai, {Shih Chong} and Pasumarthi, {Kishore B S} and Laura Pajak and Michael Franklin and Brian Patton and He Wang and Henzel, {William J.} and Stults, {John T.} and Loren Field",
year = "2000",
month = "2",
day = "4",
doi = "10.1074/jbc.275.5.3239",
language = "English",
volume = "275",
pages = "3239--3246",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "5",

}

TY - JOUR

T1 - Simian virus 40 large T antigen binds a novel Bcl-2 homology domain 3- containing proapoptosis protein in the cytoplasm

AU - Tsai, Shih Chong

AU - Pasumarthi, Kishore B S

AU - Pajak, Laura

AU - Franklin, Michael

AU - Patton, Brian

AU - Wang, He

AU - Henzel, William J.

AU - Stults, John T.

AU - Field, Loren

PY - 2000/2/4

Y1 - 2000/2/4

N2 - A 193-kDa SV40 large T antigen (T-Ag)-binding protein, designated p193, was identified and cloned. Inspection of the deduced amino acid sequence revealed the presence of a short motif similar to the Bcl-2 homology (BH) domain 3, suggesting that p193 may be a member of a family of apoptosis promoting proteins containing only BH3 motifs. In support of this, p193 expression promoted apoptosis in NIH-3T3 cells. Deletion of the BH3 motif abolished p193 apoptosis activity, p193-induced apoptosis was antagonized by co-expression of Bcl-X(L). Immune cytologic analysis indicated that p193 is localized to the cytoplasm of transfected cells, p193-induced apoptosis was also antagonized by co-expression of T-Ag, which resulted in the cytoplasmic localization of both proteins. The p193 binding site was mapped to an N- terminal region of T-Ag previously implicated in transforming activity. These results suggest that T-Ag possesses an antiapoptosis activity, independent of p53 sequestration, which is actuated by T-Ag/p193 binding in the cytoplasm.

AB - A 193-kDa SV40 large T antigen (T-Ag)-binding protein, designated p193, was identified and cloned. Inspection of the deduced amino acid sequence revealed the presence of a short motif similar to the Bcl-2 homology (BH) domain 3, suggesting that p193 may be a member of a family of apoptosis promoting proteins containing only BH3 motifs. In support of this, p193 expression promoted apoptosis in NIH-3T3 cells. Deletion of the BH3 motif abolished p193 apoptosis activity, p193-induced apoptosis was antagonized by co-expression of Bcl-X(L). Immune cytologic analysis indicated that p193 is localized to the cytoplasm of transfected cells, p193-induced apoptosis was also antagonized by co-expression of T-Ag, which resulted in the cytoplasmic localization of both proteins. The p193 binding site was mapped to an N- terminal region of T-Ag previously implicated in transforming activity. These results suggest that T-Ag possesses an antiapoptosis activity, independent of p53 sequestration, which is actuated by T-Ag/p193 binding in the cytoplasm.

UR - http://www.scopus.com/inward/record.url?scp=0034603002&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034603002&partnerID=8YFLogxK

U2 - 10.1074/jbc.275.5.3239

DO - 10.1074/jbc.275.5.3239

M3 - Article

C2 - 10652310

AN - SCOPUS:0034603002

VL - 275

SP - 3239

EP - 3246

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 5

ER -