The SV40 transcription complex. II. Non-dissociation of protein from SV40 chromatin during transcription

Green, Melvin H.; Brooks, Timothy L.

doi:10.1093/nar/4.12.4279

Cited by 25 publications

(9 citation statements)

References 27 publications

(34 reference statements)

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“…However, it is possible that histones remain on the active chromatin but simply rearrange to a structure which does not yield the usual repeat pattern. This is consistent with the reversibility of the altered pattern (1,2), with earlier biochemical data which suggests subtle alterations in the structure of "active" chromatin (reviewed 3) and with suggestions from RNA synthetic experiments that transcription can occur without histone dissociation (5)(6)(7)(8). Also, Moyne et al.…”

Section: Introductionsupporting

confidence: 89%

The chromatin structure of an actively expressed, single copy yeast gene

Lohr

1983

Nucl Acids Res

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When the yeast galactokinase gene is not active (repressed, not expressed, quiescent), there is an exceptionally regular nucleosome array on coding sequence galactokinase chromatin, as shown by both denaturing and non-denaturing gel analysis of staphylococcal nuclease digests. Expression of the gene results in a limited smearing of the nucleosome repeat peaks and an increase in interpeak DNA, appearing as a regular ladder of DNA bands on denaturing gels. On non-denaturing gels the pattern is more complex and molecular weight dependent. These data suggest an increase in intracore particle DNA accessibility, allowing staphylococcal nuclease to digest throughout the nucleosome in expressed chromatin. Comparison to bulk chromatin and to an operationally inactive gene (35S rDNA) show that the alteration is specific to expressed chromatin. In contrast, DNase I shows no differences in the digestion of the gene specific chromatin in expressed or inactive states.

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Section: Introductionsupporting

confidence: 89%

The chromatin structure of an actively expressed, single copy yeast gene

Lohr

1983

Nucl Acids Res

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“…About 0.5 to 1% of the total viral DNA extracted from nuclei with Triton X-100 or Sarkosyl is engaged in complexes with RNA polymerase II (36). Under optimal conditions in vitro, Triton X-100 complexes can synthesize RNA chains much longer than the viral genome, without irreversible alteration of the chromatin-like structure (7,19,24). As with Sarkosyl complexes, about 95% of the RNA made from Triton X-100 complexes isolated late in infection is complementary to the late DNA strand (23).…”

Section: Discussionmentioning

confidence: 99%

Two deletions within genes for simian virus 40 structural proteins VP2 and VP3 lead to formation of abnormal transcriptional complexes

Llopis

Stark

1981

J Virol

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The procedure developed by R. M. Fernandez-Mufioz et al. (J. Virol. 29:612-623, 1979) for isolating simian virus 40 (SV40) chromatin free of disrupted previrions was optimized for preparing late transcriptional complexes, and these complexes were partially characterized. Transcriptional complexes derived from wild-type virus and from several deletion and temperature-sensitive mutants could be activated more than five-fold either by the anionic detergent Sarkosyl or by 300 mM ammonium sulfate, in agreement with the properties of SV40 transcriptional complexes prepared by other procedures. In contrast, complexes from cells infected with deletion mutants d11261 or d11262 were not activated at all by a high salt concentration, even though the extent of their activation by Sarkosyl was normal. Mutants d11261 and d11262 carry deletions of 54 and 36 base pairs, respectively, at an approximate map position of 0.91, which is within the overlapping genes for the virion proteins VP2 and VP3. The effects of these deletions on transcription in vitro indicate that VP2 or VP3 or both are bound to late transcriptional complexes in a way that affects the progress of initiated RNA polymerase. The properties of late transcriptional complexes derived from wildtype SV40 can be explained by the presence of the following two different kinds of complexes: (i) a minority class (about 20%), which is free of VP2 or VP3, active at low concentrations of ammonium sulfate in vitro, and responsible for late transcription in vivo, and (ii) a majority class (about 80%) with VP2 or VP3 bound, which is inactive at low salt concentrations both in vitro and in vivo but capable of being activated by high salt concentrations or by Sarkosyl. We propose that mutant VP2 and VP3 proteins from d11261 and d11262 bind to the majority class of late transcriptional complexes in a way that can be reversed by Sarkosyl but not by a high salt concentration.

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“…Since practically all of the viral DNA is found in these nucleoprotein complexes at all stages of the viral cycle (3)(4)(5)(6), it is very suggestive to think that actual transcription of papovavirus DNA in the infected cell occurs on such templates rather than on "naked" DNA. These viral chromatins, called by some authors "minichromosomes" (1-3), were in fact isolated from infected cells and studied as templates for endogenously catalyzed transcription (18)(19)(20)(21). In those studies, however, only a small fraction (less than one per cent) of the minichromosomes were transcriptionally active, making the precise nature of the template somewhat uncertain.…”

Section: Discussionmentioning

confidence: 99%