Bovine papilloma virus-transformed cells contain multiple E2 proteins

N. L. Hubbert, J. T. Schiller, D. R. Lowy, Elliot Androphy

Research output: Contribution to journalArticle

62 Citations (Scopus)

Abstract

Genetic evidence suggests that the bovine papilloma virus type 1 (BPV) E2 open reading frame may encode at least two gene products involved in the regulation of viral gene expression. One, which is probably the full-length product, trans-activates transcription via an enhancer in the viral regulatory region. A second, containing sequences from the 3' end of the open reading frame, inhibits the transactivating activity of the first product. We now report the identification and initial characterization of three E2-encoded proteins, with mobilities corresponding to 48, 31, and 28 kDa in cells transformed by the wild-type BPV. Pulse-chase experiments indicated that the 48-kDa protein had the longest half-life (40 min), but there was no indication that one species was the precursor of another. The 48-kDa species corresponds to the full-length trans-activating protein. The two smaller species contain only carboxyl-terminal determinants, and either or both could represent inhibitory E2 proteins. Subcellular fractionation localized all three E2 proteins to the nucleus. Consistent with the low rate of viral transcription in BPV-transformed cells, the 31-kDa presumptive repressor species was more abundant than the 48-kDa species.

Original languageEnglish (US)
Pages (from-to)5864-5868
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume85
Issue number16
StatePublished - 1988
Externally publishedYes

Fingerprint

Papilloma
Viruses
Proteins
Open Reading Frames
Viral Gene Expression Regulation
Nucleic Acid Regulatory Sequences
Half-Life
Genes

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

Bovine papilloma virus-transformed cells contain multiple E2 proteins. / Hubbert, N. L.; Schiller, J. T.; Lowy, D. R.; Androphy, Elliot.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 85, No. 16, 1988, p. 5864-5868.

Research output: Contribution to journalArticle

@article{6fa1caf0203548209296c51989d4b2a4,
title = "Bovine papilloma virus-transformed cells contain multiple E2 proteins",
abstract = "Genetic evidence suggests that the bovine papilloma virus type 1 (BPV) E2 open reading frame may encode at least two gene products involved in the regulation of viral gene expression. One, which is probably the full-length product, trans-activates transcription via an enhancer in the viral regulatory region. A second, containing sequences from the 3' end of the open reading frame, inhibits the transactivating activity of the first product. We now report the identification and initial characterization of three E2-encoded proteins, with mobilities corresponding to 48, 31, and 28 kDa in cells transformed by the wild-type BPV. Pulse-chase experiments indicated that the 48-kDa protein had the longest half-life (40 min), but there was no indication that one species was the precursor of another. The 48-kDa species corresponds to the full-length trans-activating protein. The two smaller species contain only carboxyl-terminal determinants, and either or both could represent inhibitory E2 proteins. Subcellular fractionation localized all three E2 proteins to the nucleus. Consistent with the low rate of viral transcription in BPV-transformed cells, the 31-kDa presumptive repressor species was more abundant than the 48-kDa species.",
author = "Hubbert, {N. L.} and Schiller, {J. T.} and Lowy, {D. R.} and Elliot Androphy",
year = "1988",
language = "English (US)",
volume = "85",
pages = "5864--5868",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "16",

}

TY - JOUR

T1 - Bovine papilloma virus-transformed cells contain multiple E2 proteins

AU - Hubbert, N. L.

AU - Schiller, J. T.

AU - Lowy, D. R.

AU - Androphy, Elliot

PY - 1988

Y1 - 1988

N2 - Genetic evidence suggests that the bovine papilloma virus type 1 (BPV) E2 open reading frame may encode at least two gene products involved in the regulation of viral gene expression. One, which is probably the full-length product, trans-activates transcription via an enhancer in the viral regulatory region. A second, containing sequences from the 3' end of the open reading frame, inhibits the transactivating activity of the first product. We now report the identification and initial characterization of three E2-encoded proteins, with mobilities corresponding to 48, 31, and 28 kDa in cells transformed by the wild-type BPV. Pulse-chase experiments indicated that the 48-kDa protein had the longest half-life (40 min), but there was no indication that one species was the precursor of another. The 48-kDa species corresponds to the full-length trans-activating protein. The two smaller species contain only carboxyl-terminal determinants, and either or both could represent inhibitory E2 proteins. Subcellular fractionation localized all three E2 proteins to the nucleus. Consistent with the low rate of viral transcription in BPV-transformed cells, the 31-kDa presumptive repressor species was more abundant than the 48-kDa species.

AB - Genetic evidence suggests that the bovine papilloma virus type 1 (BPV) E2 open reading frame may encode at least two gene products involved in the regulation of viral gene expression. One, which is probably the full-length product, trans-activates transcription via an enhancer in the viral regulatory region. A second, containing sequences from the 3' end of the open reading frame, inhibits the transactivating activity of the first product. We now report the identification and initial characterization of three E2-encoded proteins, with mobilities corresponding to 48, 31, and 28 kDa in cells transformed by the wild-type BPV. Pulse-chase experiments indicated that the 48-kDa protein had the longest half-life (40 min), but there was no indication that one species was the precursor of another. The 48-kDa species corresponds to the full-length trans-activating protein. The two smaller species contain only carboxyl-terminal determinants, and either or both could represent inhibitory E2 proteins. Subcellular fractionation localized all three E2 proteins to the nucleus. Consistent with the low rate of viral transcription in BPV-transformed cells, the 31-kDa presumptive repressor species was more abundant than the 48-kDa species.

UR - http://www.scopus.com/inward/record.url?scp=0023755030&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023755030&partnerID=8YFLogxK

M3 - Article

VL - 85

SP - 5864

EP - 5868

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 16

ER -