Polyoma virus DNA replication requires an enhancer

Villiers, Jean de; Schaffner, Walter; Tyndall, Chiara; Lupton, S; Kamen, Robert

doi:10.1038/312242a0

Cited by 250 publications

(184 citation statements)

References 49 publications

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“…Direct repeat structures have been found in many enhancers, and duplications generally increase enhancer activity (Weber et al, 1984;de Villiers et al, 1983de Villiers et al, , 1984.…”

Section: What Elements Make Up An Enhancer?mentioning

confidence: 99%

A very strong enhancer is located upstream of an immediate early gene of human cytomegalovirus

Boshart

Weber

Jahn

et al. 1985

Cell

1,097

648

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SummaryA strong transcription enhancer was identified in the genomic DNA (235 kb) of human cytomegalovirus (HCMV), a ubiquitous and severe pathogen of the herpesvirus group. Cotransfection of enhancerless SV40 DNA with randomly fragmented HCMV DNA yielded two SV40-HCMV recombinant viruses that had incorporated overlapping segments of HCMV DNA to substitute for the missing SV40 enhancer. Within HCMV, these enhancer sequences are located upstream of the transcription initiation site of the major immediate-early gene, between nucleotides -118 and -524. Deletion studies with the HCMV enhancer, which harbors a variety of repeated sequence motifs, show that different subsets of this enhancer can substitute for the SV40 enhancer. The HCMV enhancer, which seems to have little cell type or species preference, is severalfold more active than the SV40 enhancer. It is the strongest enhancer we have analyzed so far, a property that makes it a useful component of eukaryotic expression vectors.

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“…Direct repeat structures have been found in many enhancers, and duplications generally increase enhancer activity (Weber et al, 1984;de Villiers et al, 1983de Villiers et al, , 1984.…”

Section: What Elements Make Up An Enhancer?mentioning

confidence: 99%

A very strong enhancer is located upstream of an immediate early gene of human cytomegalovirus

Boshart

Weber

Jahn

et al. 1985

Cell

1,097

648

View full text Add to dashboard Cite

show abstract

“…This finding is particularly interesting because it extends earlier findings and seems to generalize the link between transcription factors and DNA replication. For a few years it has been known that an enhancer is required in cis for polyoma virus DNA replication [144], and a factor facilitating adenovirus replication in vitro, designated NF-3, turned out to bind also to enhancer and promoter regions [145 -1471.…”

Section: The Same Dna Sequence Motif (Octamer) As Well As General Tramentioning

confidence: 99%

Enhancer sequences and the regulation of gene transcription

Müller

Gerster

Schaffner

1988

European Journal of Biochemistry

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151

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“…Several reports about proteins interacting with enhancer sequences have been published recently (16,17,18,19,20,21). The enhancer of polyoma virus that is studied here is necessary both for transcription from the early promoter and for the replication of viral DNA (22,23,24). It could be subdivided into two fragments conserving partial activity: the PvuII-BclI fragment or A enhancer and the PvuII-4 fragment or B enhancer (25).…”

Section: Intkroduionmentioning

confidence: 99%

Molecular analysis of the interaction between an enhancer binding factor and its DNA target

Piette

Yaniv

1986

Nucl Acids Res

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ABSTRATTIei fine contacts of a mouse nuclear factor, called PEB1, with the B enhancer of polyoma virus were analyzed. It protects against DNaseI attack a region of about 50 base pairs that can be divided in two domains. The first contains a GC-rich palindrome and the homology to the SV40 enhancer. The second is homologous to a sequence in the immunoglobulin (Ig) heavy chain gene enhancer. Methylation interference and protection experiments reveal strong specific contacts only with a purine rich track on the late coding strand of the early proximal part of the palindrome. Deletion analysis show that the minimal sequences necessary for binding include only the first domain. The Ig homology contributes only weakly to the binding. The minimal core is similar to the core of the B enhancer defined in vivo. The interactions we observe here are reminiscent of those of TFIIIA positive transcription factor and the 5SRNA gene of Xenopus. INTKRODUIONDNA-protein interactions play an essential role in the regulation of gene expression and DNA replication. Characterization of these interactions can help unravel the mechanisms involved in these processes. Repressor-operator interactions in prokaryotes were the first to be analyzed in great detail: in essence, a repressor dimer interacts with both parts of a palindromic sequence in a symmetric way; a conserved c-helix-turn-a-helix motif fits into the large groove of right-handed B-DNA (1). This model was found to be applicable to activator proteins like the CAP protein (2) or even yeast proteins involved in mating type control (3).In higher eukaryotes only a few cases of specific DNA-protein interactions have been studied in detail so far. The positive transcription factor TF III A of Xenopus laevis contacts the DNA mainly along the non coding strand (4) and the helical configuration of the DNA may be altered by this binding (5). Knowledge of the primary structure of the protein has led to a model in which small Zn++ binding, fingerlike domains interact with the DNA in a way quite different from bacterial repressors or activators (6). Another

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Polyoma virus DNA replication requires an enhancer

Cited by 250 publications

References 49 publications

A very strong enhancer is located upstream of an immediate early gene of human cytomegalovirus

A very strong enhancer is located upstream of an immediate early gene of human cytomegalovirus

Enhancer sequences and the regulation of gene transcription

Molecular analysis of the interaction between an enhancer binding factor and its DNA target

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