Evidence map›Paper›PMID 1831535›Full record

ArticleMolecular and cellular biology1991

trans-dominant mutants of E1A provide genetic evidence that the zinc finger of the trans-activating domain binds a transcription factor.

L C Webster, R P Ricciardi

Abstract read
In one paragraph

Article in Molecular and cellular biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

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0cells of the map it votes in
46citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

46 citing papers in PubMed.

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  15. Activation domain-mediator interactions promote transcription preinitiation complex assembly on promoter DNA.Proceedings of the National Academy of Sciences of the United States of America · 2003
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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

2 authors.

L C WebsterWistar Institute of Anatomy and Biology, Philadelphia, Pennsylvania 19104.
R P Ricciardi

Funding

TRAINING PROGRAM IN BASIC CANCER RESEARCHT32CA009171 · NCI · WISTAR INSTITUTE · PI Alessandro Gardini · 1985 to 2026
$15.3M
ORGANIZATION &EXPRESSION OF ADENOVIRUS GENESR01CA029797 · NCI · WISTAR INSTITUTE · PI RICCIARDI, ROBERT PAUL · 1985 to 2006
$2.2M
NCI NIH HHS CA-09171NCI NIH HHS CA-29797
6 · The paper itself

Abstract

The 289R E1A protein of adenovirus stimulates transcription of early viral and certain cellular genes. trans-Activation requires residues 140 to 188, which encompass a zinc finger. Several studies have indicated that trans-activation by E1A is mediated through cellular transcription factors. In particular, the ability of the trans-dominant E1A point mutant hr5 (Ser-185 to Asn) to inhibit wild-type E1A trans-activation was proposed to result from the sequestration of a cellular factor. Using site-directed mutagenesis, we individually replaced every residue within and flanking the trans-activating domain with a conservative amino acid, revealing 16 critical residues. Six of the individual substitutions lying in a contiguous stretch C terminal to the zinc finger (carboxyl region183-188) imparted a trans-dominant phenotype. trans-Dominance was even produced by deletion of the entire carboxyl region183-188. Conversely, an intact finger region147-177 was absolutely required for trans-dominance, since second-site substitution of every critical residue in this region abrogated the trans-dominant phenotype of the hr5 protein. These data indicate that the finger region147-177 bind a limiting cellular transcription factor and that the carboxyl region183-188 provides a separate and essential function. In addition, we show that four negatively charged residues within the trans-activating domain do not comprise a distinct acidic activating region. We present a model in which the trans-activating domain of E1A binds to two different cellular protein targets through the finger and carboxyl regions.

Indexed as

Zinc FingersAdenovirus Early ProteinsAmino Acid SequenceBlotting, WesternGenes, DominantHeLa CellsHumansModels, GeneticMolecular Sequence DataMutationOncogene Proteins, ViralProtein ConformationTrans-ActivatorsAdenovirus Early ProteinsOncogene Proteins, ViralTrans-Activators

Identifiers

PMID1831535
PMCPMC361289

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.