Specific binding and protection of form II SV40 deoxyribonucleic acid by ribonucleic acid polymerase II from wheat germ

Chandler, Donald Walt; Gralla, Jay D.

doi:10.1021/bi00549a012

Cited by 39 publications

(22 citation statements)

References 50 publications

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“…SEIDMAN et al (11) have reported that these complexes are formed at or near sites at which transcription is initiated "in vivo". However, recent evidence suggest that transcription observed in the presence of heparin does not reflect initiation at specific sites, but rather at single-strand breaks (13,14,15 (16) was cut at its unique Sal I site and was cloned in the Sal I site of plasmid pAT 153 (17). One of the hybrid plasmids, pMD 125, containing a full length gename, was selected and used in the experiments described in this paper.…”

Section: Introductionmentioning

confidence: 99%

Electron microscopic mapping of wheat germ RNA polymerase II binding sites on cloned CaMV DNA

Grellet

Cooke

Teissere³

et al. 1981

Nucl Acids Res

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The binding sites of wheat germ RNA polymerase II were mapped on the cloned CaMV genome by observation of enzyme-linear DNA complexes by electron microscopy. Twelve sites are observed. Three of them are relatively stable in the presence of heparin and are found at positions8-9, 21-23, and 41-44 map units on the physical map of the genome. These positions correspond to ATrich regions of the viral genome which contain potential promoter sites. These results are discussed with reference to current information on the structure and expression of the CaMV genome.

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Section: Introductionmentioning

confidence: 99%

Electron microscopic mapping of wheat germ RNA polymerase II binding sites on cloned CaMV DNA

Grellet

Cooke

Teissere³

et al. 1981

Nucl Acids Res

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“…The site of nicking is in fact specifically bound and protected from nuclease digestion by RNA polymerase II (7). N complexes form rapidly, are very long-lived, and are , on the average, transcriptionally competent.…”

Section: Discussionmentioning

confidence: 99%

“…However Previously, we reported that wheat germ RNA polymerase II binds principally to nicks when present in SV40 DNA (7) and that the complex formed is sufficiently stable to provide protection from nuclease attack. Figure 6 shows a direct measure of stability of a complex formed by the wheat germ enzyme at a nick introduced at 0.725 map units on the SV40 genome.…”

Section: Methodsmentioning

confidence: 99%

“…Cells, SV40 virus, and supercoiled DNA were prepared as described previously (7). 3H SV40 DNA was isolated from cells labeled by the addition of 10i Ci of tritiated thymidine per ml of media 24 hours after infection.…”

Section: Methodsmentioning

confidence: 99%

“…RNA polymerase II from wheat germ has been shown to bind preferentially near single strand breaks in DNA (7) and heparin-resistant transcription also arises preferentially from nick sites (5). Restriction cleavage of DNA may also lead to single strand breaks (8).…”

Section: Introductionmentioning

confidence: 99%

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The interaction of RNA polymerase II with non-promoter DNA sites

Chandler¹,

Gralla²

1981

Nucl Acids Res

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Various complexes formed between purified RNA polymerase II and simian virus 40 DNA have been characterized with respect to rates of formation, rates of dissociation, and initial velocity of RNA synthesis. Two different types of complexes can form on intact DNA templates. One of these is formed rapidly, but is quite labile; the other forms more slowly, but is moderately stable once formed. The introduction of a single strand break into DNA leads to rapid and stable complex formation, and thus is expected to create the favored binding site.The observed properties of these complexes provide a general framework for describing the interactions of RNA polymerase II at non-promoter DNA sites. This framework appears to be similar to that established for Escherichia coli RNA polymerase interactions, suggesting that the fundamental mode of non-promoter DNA binding is similar for the bacterial, plant, and mammalian enzymes.

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Enzymatic properties of plant RNA polymerases

Cooke

Durand²,

Job³

et al. 1984

Plant Mol Biol

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Results obtained in the past few years in the study of the reaction mechanism of plant RNA polymerases are reviewed and discussed. They suggest that valuable information can be obtained using a highly simplified transcription system composed of purified plant enzymes and cloned genes. This type of approach may provide a starting point for the development of an in vitro transcription system. The detailed study of the fundamental enzymatic properties of the plant RNA polymerases allows a comparison with the well documented corresponding bacterial enzyme.

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Specific binding and protection of form II SV40 deoxyribonucleic acid by ribonucleic acid polymerase II from wheat germ

Cited by 39 publications

References 50 publications

Electron microscopic mapping of wheat germ RNA polymerase II binding sites on cloned CaMV DNA

Electron microscopic mapping of wheat germ RNA polymerase II binding sites on cloned CaMV DNA

The interaction of RNA polymerase II with non-promoter DNA sites

Enzymatic properties of plant RNA polymerases

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