Factors Influencing the Activity of Mammalia RNA Polymerase

Stein, Hans; Hausen, Peter

doi:10.1101/sqb.1970.035.01.086

Cited by 39 publications

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“…Factors which specifically stimulate transcription by R N A polymerase I1 on double-stranded D N A templates have been identified in extracts of calf thymus (Stein & Hausen, 1970) and rat liver (Seifart, 1970;Seifart et al, i972), KB cells (Sugden & Keller, 1973), Novikoff ascites cells (Lee & Dahmus, 1973), and mouse-myeloma cells (Lentfer & Lezius, 1972). These factors stimulate homologous R N A polymerase 11 four-to tenfold on native DNA but do not stimulate the activity of R N A polymerase I or E .…”

Section: Dna-dependent R N a Polymerase I1 Stimulatory Factors From Cmentioning

confidence: 99%

DNA-dependent RNA polymerase II stimulatory factors from calf thymus: purification and structural studies

Rh¹,

Spindler²,

Hg³

et al. 1978

Biochemistry

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Protein factors which stimulate R N A polymerase I1 but not polymerases I and 111 on native D N A have been isolated from calf thymus. These factors are basic proteins and exhibit properties which are similar to the stimulatory factor first described by H. Stein & P. Hausen [(1971) Cold Spring Harbor Symp. Quant. Biol. 35, 7 191. The stimulatory factors are initially purified by the following steps: homogenization, 40-80% ammonium sulfate precipitation, DEAE-Sephadex, CM-cellulose, and Sephadex G-75. Two stimulatory peaks (SF-1 and SF-2) are resolved by Sephadex G-75. SF-1 is resistant while SF-2 is sensitive to heat denaturation at 98 'C. The protein kinase activity present in SF-1 is heat labile, demonstrating that it is not responsible for the stimulation by SF-1. Both factors stimulate transcription on native calf thymus DNA but not denatured calf thymus DNA. SF-2 stimulates while SF-I does not stimulate transcription on poly[d(A-T)]. Both factors are sensitive to digestion with proteolytic enzymes, indicating that both factors contain a protein which is essential for stimulatory activity. Gel filtration studies show that SF-1 and SF-2 exhibit native molecular weights of D i f f e r e n t classes of eukaryotic RNA polymerase (Roeder and Rutter, 1969) transcribe the respective classes of cellular RNA. R N A polymerase

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Section: Dna-dependent R N a Polymerase I1 Stimulatory Factors From Cmentioning

confidence: 99%

DNA-dependent RNA polymerase II stimulatory factors from calf thymus: purification and structural studies

Rh¹,

Spindler²,

Hg³

et al. 1978

Biochemistry

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“…At present, this is the only stimulatory factor extractable from animal tissues, for which formation of a complex between factor and the sensitive enzyme has been reported [2]. This complex formation appears to be specific in so far, as it is restricted to the RNA polymerase B.…”

Section: Introductionmentioning

confidence: 99%

“…The previously defined fraction S of calf thymus contains a basic protein factor which efficiently stimulates the activity of the eucaryotic cY-amanitin sensitive RNA polymerase B (or II) on a native DNA template under defined in vitro conditions [ 1,2]. At present, this is the only stimulatory factor extractable from animal tissues, for which formation of a complex between factor and the sensitive enzyme has been reported [2].…”

Section: Introductionmentioning

confidence: 99%

The role of basic proteins in the DNA dependent RNA polymerase reaction

Brand¹,

Spindler²,

Stein³

1977

FEBS Letters

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“…Since RNA polymerase content and character were essentially the same in infected and uninfected cells, we examined alternative explanations for the effects of in fection on RNA synthesis. Reports [23][24][25][26][27][28][29] that protein factors that stimulate eucaryotic RNA polymerase activity pass through DEAE-Sephadex under conditions where enzyme is retained, prompted our investigation of these column fractions in infected cell extracts. Samples of the fractions that washed through the DEAE-Sephadex columns (WTF) were tested for their influence on the two peaks of RNA polymerases from infected and uninfected cells.…”

Section: Resultsmentioning

confidence: 99%

“…For purposes of experimental design, we have considered this protein to be a 'factor' analogous to activation factors previously described [23][24][25][26][27][28][29]. Further purification of the inhibitor was not at tempted, but properties of the inhibitory 'factor' eluted from CM-Sephadex were determined.…”

Section: Characteristics O F the Inhibition O F Rna Polymerasementioning

confidence: 99%

RNA Polymerase Activity and Inhibition in Herpesvirus-Infected Cells

Sasaki¹,

Sasaki²,

Cohen³

et al. 1974

Intervirology

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The activity of the DNA-dependent RNA polymerase (ribonucleotide tri-phosphate:RNA nucleotidyl transferase, EC 2.7.7.6) was present but not proportional to protein concentration in unfractionated extracts of KB cells infected with herpes simplex virus. Chromatography on DEAE-Sephadex demonstrated two peaks of enzyme activity in infected cell extracts that had properties indistinguishable from the enzymes present in uninfected cells and an inhibitor of RNA polymerase activity that was not retained by the DEAE-Sephadex. The inhibitor was not present in uninfected cell extracts and was not formed if protein synthesis was blocked with cyclohexamide at the time of infection. The inhibitor could be partially purified by CM-Sephadex chromatography; it preferentially inhibited the nucleolar enzyme (peak I) and acted by stopping chain elongation. It is probable that this inhibitor of RNA polymerase participates in the reduction of cellular RNA synthesis observed after herpesvirus infection.

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Factors Influencing the Activity of Mammalia RNA Polymerase

Cited by 39 publications

References 0 publications

DNA-dependent RNA polymerase II stimulatory factors from calf thymus: purification and structural studies

DNA-dependent RNA polymerase II stimulatory factors from calf thymus: purification and structural studies

The role of basic proteins in the DNA dependent RNA polymerase reaction

RNA Polymerase Activity and Inhibition in Herpesvirus-Infected Cells

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