p300 Family members associate with the carboxyl terminus of simian virus 40 large tumor antigen

Nancy Lill, Mary Judith Tevethia, Richard Eckner, David M. Livingston, Nazanine Modjtahedi

Research output: Contribution to journalArticle

71 Citations (Scopus)

Abstract

Several cellular polypeptides critical for growth regulation interact with DNA tumor virus oncoproteins. p400 is a cellular protein which binds to the adenovirus E1A oncoprotein(s). The biological function of p400 is not yet known, but it is structurally and immunologically closely related to p300 and CREB-binding protein, two known E1A-binding transcription adapters. Like p300, p400 is a phosphoprotein that binds to the simian virus 40 large tumor antigen (T). In anti-T coimmunoprecipitation experiments, staggered deletions spanning the amino-terminal 250 amino acids of T did not abrogate T binding to either p400 or p300. A T species composed of residues 251 to 708 bound both p400 and p300, while a T species defective in p53 binding was unable to bind either detectably. Anti-p53 immunoprecipitates prepared from cells containing wild-type T also contained p400 and p300. Hence, both p400 and p300 can bind (directly or indirectly) to a carboxyl-terminal fragment of T which contains its p53 binding domain. Since the p53 binding domain of T contributes to its immortalizing and transforming activities, T-p400 and/or T-p300 interactions may participate in these functions.

Original languageEnglish (US)
Pages (from-to)129-137
Number of pages9
JournalJournal of virology
Volume71
Issue number1
StatePublished - Jan 1 1997

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Simian virus 40
Oncogene Proteins
Neoplasm Antigens
DNA Tumor Viruses
CREB-Binding Protein
antigens
phosphoproteins
neoplasms
Phosphoproteins
Viral Tumor Antigens
Adenoviridae
binding proteins
polypeptides
transcription (genetics)
Amino Acids
viruses
Peptides
amino acids
DNA
Growth

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

Cite this

Lill, N., Tevethia, M. J., Eckner, R., Livingston, D. M., & Modjtahedi, N. (1997). p300 Family members associate with the carboxyl terminus of simian virus 40 large tumor antigen. Journal of virology, 71(1), 129-137.
Lill, Nancy ; Tevethia, Mary Judith ; Eckner, Richard ; Livingston, David M. ; Modjtahedi, Nazanine. / p300 Family members associate with the carboxyl terminus of simian virus 40 large tumor antigen. In: Journal of virology. 1997 ; Vol. 71, No. 1. pp. 129-137.
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abstract = "Several cellular polypeptides critical for growth regulation interact with DNA tumor virus oncoproteins. p400 is a cellular protein which binds to the adenovirus E1A oncoprotein(s). The biological function of p400 is not yet known, but it is structurally and immunologically closely related to p300 and CREB-binding protein, two known E1A-binding transcription adapters. Like p300, p400 is a phosphoprotein that binds to the simian virus 40 large tumor antigen (T). In anti-T coimmunoprecipitation experiments, staggered deletions spanning the amino-terminal 250 amino acids of T did not abrogate T binding to either p400 or p300. A T species composed of residues 251 to 708 bound both p400 and p300, while a T species defective in p53 binding was unable to bind either detectably. Anti-p53 immunoprecipitates prepared from cells containing wild-type T also contained p400 and p300. Hence, both p400 and p300 can bind (directly or indirectly) to a carboxyl-terminal fragment of T which contains its p53 binding domain. Since the p53 binding domain of T contributes to its immortalizing and transforming activities, T-p400 and/or T-p300 interactions may participate in these functions.",
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Lill, N, Tevethia, MJ, Eckner, R, Livingston, DM & Modjtahedi, N 1997, 'p300 Family members associate with the carboxyl terminus of simian virus 40 large tumor antigen', Journal of virology, vol. 71, no. 1, pp. 129-137.

p300 Family members associate with the carboxyl terminus of simian virus 40 large tumor antigen. / Lill, Nancy; Tevethia, Mary Judith; Eckner, Richard; Livingston, David M.; Modjtahedi, Nazanine.

In: Journal of virology, Vol. 71, No. 1, 01.01.1997, p. 129-137.

Research output: Contribution to journalArticle

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N2 - Several cellular polypeptides critical for growth regulation interact with DNA tumor virus oncoproteins. p400 is a cellular protein which binds to the adenovirus E1A oncoprotein(s). The biological function of p400 is not yet known, but it is structurally and immunologically closely related to p300 and CREB-binding protein, two known E1A-binding transcription adapters. Like p300, p400 is a phosphoprotein that binds to the simian virus 40 large tumor antigen (T). In anti-T coimmunoprecipitation experiments, staggered deletions spanning the amino-terminal 250 amino acids of T did not abrogate T binding to either p400 or p300. A T species composed of residues 251 to 708 bound both p400 and p300, while a T species defective in p53 binding was unable to bind either detectably. Anti-p53 immunoprecipitates prepared from cells containing wild-type T also contained p400 and p300. Hence, both p400 and p300 can bind (directly or indirectly) to a carboxyl-terminal fragment of T which contains its p53 binding domain. Since the p53 binding domain of T contributes to its immortalizing and transforming activities, T-p400 and/or T-p300 interactions may participate in these functions.

AB - Several cellular polypeptides critical for growth regulation interact with DNA tumor virus oncoproteins. p400 is a cellular protein which binds to the adenovirus E1A oncoprotein(s). The biological function of p400 is not yet known, but it is structurally and immunologically closely related to p300 and CREB-binding protein, two known E1A-binding transcription adapters. Like p300, p400 is a phosphoprotein that binds to the simian virus 40 large tumor antigen (T). In anti-T coimmunoprecipitation experiments, staggered deletions spanning the amino-terminal 250 amino acids of T did not abrogate T binding to either p400 or p300. A T species composed of residues 251 to 708 bound both p400 and p300, while a T species defective in p53 binding was unable to bind either detectably. Anti-p53 immunoprecipitates prepared from cells containing wild-type T also contained p400 and p300. Hence, both p400 and p300 can bind (directly or indirectly) to a carboxyl-terminal fragment of T which contains its p53 binding domain. Since the p53 binding domain of T contributes to its immortalizing and transforming activities, T-p400 and/or T-p300 interactions may participate in these functions.

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Lill N, Tevethia MJ, Eckner R, Livingston DM, Modjtahedi N. p300 Family members associate with the carboxyl terminus of simian virus 40 large tumor antigen. Journal of virology. 1997 Jan 1;71(1):129-137.