Transcription in Yeast: A Factor that Stimulates Yeast RNA Polymerases

Mauro, Ernesto Di; Hollenberg, Cornelis P.; Hall, Benjamin D.

doi:10.1073/pnas.69.10.2818

Cited by 28 publications

(5 citation statements)

References 18 publications

(13 reference statements)

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“…The non-histone chromosomal protein fraction was also devoid of contaminating nuclease activity; this was shown as described by Di Mauro et al (1972).…”

Section: Methodsmentioning

confidence: 62%

“…Many examples of more or less purified protein factors that stimulate RNA synthesis in vitro have been reported (Stein & Hausen, 1970;Jacquet et al, 1971;Di Mauro et al, 1972;Lee & Dahmus, 1973;Seifart et al, 1973;Sudgen & Keller, 1973;Teissere et al, 1975). Some exhibit pronounced enzyme specificity and have much greater stimulatory effect on eukaryotic RNA polymerase form B (Stein & Hausen, 1970;Seifart et al, 1973;Sudgen & Keller, 1973).…”

Section: Discussionmentioning

confidence: 99%

“…Some exhibit pronounced enzyme specificity and have much greater stimulatory effect on eukaryotic RNA polymerase form B (Stein & Hausen, 1970;Seifart et al, 1973;Sudgen & Keller, 1973). Other factors, such as 7r-factor purified from Saccharomyces cerevisiae (Di Mauro et al, 1972), seem to stimulate some step of the transcription process that is common to a large number of enzymetemplate combinations; we have in addition observed that 7r-factor has a stimulatory-inhibitory action that depends, as for sea-urchin non-histone chromosomal proteins, on the amount of template present (Di Mauro et al, 1974). A correlation of the stimulatory activity with the excess of template has been reported also for the E. coli factor H (Jacquet et al, 1971).…”

Section: Discussionmentioning

confidence: 99%

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Effect of non-histone chromosomal proteins on transcription in vitro in sea-urchin

Mauro¹,

Pedone²,

Pomponi³

1978

Biochemical Journal

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Non-histone chromosomal proteins prepared from chromosomal material of the sea-urchin Paracentrotus lividus affect RNA synthesis in vitro. 1. The extent of transcription can be radically changed from inhibition to stimulation, depending on the DNA/non-histone chromosomal proteins ratio. 2. A correlation exists between stage of development and influence on transcription. 3. Non-histone chromosomal proteins exert their action by intervening directly on some initiation step of RNA synthesis, as shown by the numbers of initiation events that take place in their presence or absence. 4. Stimulatory activity is observed only in restrictive conditions of ionic strength and temperature. These observations are in agreement with models that predict for non-histone chromosomal proteins a regulatory role on the transcription process exerted through a modulation of promoter availability.

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“…The non-histone chromosomal protein fraction was also devoid of contaminating nuclease activity; this was shown as described by Di Mauro et al (1972).…”

Section: Methodsmentioning

confidence: 62%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Effect of non-histone chromosomal proteins on transcription in vitro in sea-urchin

Mauro¹,

Pedone²,

Pomponi³

1978

Biochemical Journal

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“…Other similar chromatin binding proteins are also capable of affecting RNA synthesis (Teng et al, 1971;Shea and Kleinsmith, 1973;Kostraba et al, 1975). A low molecular weight (12 000) stimulatory activity has been isolated from yeast (DiMauro et al, 1972). More recently, a "histone-like" nonhistone chromosomal protein has been purified from rat liver nucleoli.…”

Section: Discussionmentioning

confidence: 99%

A protein cofactor that stimulates the activity of DNA-dependent RNA polymerase I on double-stranded DNA

Goldberg¹,

Perriard²,

Rutter³

1977

Biochemistry

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Partially purified rat liver RNA polymerase I chromatographed on ribosomal RNA-Sepharose loses most (96%) of its activity assayed on native calf-thymus DNA templates, but loses little (8%) of its activity assayed on poly(deoxycytidylic acid) template. Polymerase I is not stimulated by polymerase II protein factor, or by bovine serum albumin. However, it is stimulated by histones, polylysine, and spermine. Addition of a protein fraction eluted by high ionic strength from the rRNA-Sepharose also restores activity on native calf-thymus DNA. Further purification yields a fraction containing two proteins of 11 000 and 12 000 molecular weight. Both proteins are distinct from histones by electrophoresis in sodium dodecyl sulfate and in acid urea. Both proteins are basic, insensitive to heat, bind to DNA, and stimulate polymerase I activity. The degree of stimulation of polymerase I is dependent upon both the enzyme/DNA and the factor/DNA ratio. The protein factors also stimulate polymerase II activity about half as effectively as polymerase I.

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“…On the other hand, the step increase of the activity of the RNA polymerase II in G2 cells could be due to the fluctuation during the cell cycle of a stimulatory factor. The presence of a factor which stimulates the in vitro activity of the RNA polymerases has been reported in yeast (15). To explain the results, however, this factor has to be present in the same fractions as RNA tract and it has to be in limiting amounts because, as indicated in Table 1, fractions containing the RNA polymerase II from G2 cells fail to stimulate the activity of the RNA polymerase II from S phase cells and the activity of the RNA polymerase I.…”

Section: Separation and Characterization Of The Fractions Containingmentioning

confidence: 99%

Independent Regulation of the Nuclear RNA Polymerases I and II During the Yeast Cell Cycle

Sebastián

Takano

Halvorson

1974

Proc. Natl. Acad. Sci. U.S.A.

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The activities of the nuclear RNA polymerases I and II have been investigated in cells of Saccharomyces cerevisiae at GI, S, early G2, and late G2 stages of the cell cycle. The results show that the ratio of the activities of the two enzymes is different at these four stages, indicating that the two RNA polymerases are regulated independently during the cell cycle. The specific activity of the RNA polymerase I remains conrtant but that of RNA polymerase II increases sharply in cells at the beginning' of the G2 phase. These results are compatible with a pattern of continuous synthesis of the RNA polymerase I and step-wise synthesis of the RNA polymerase II during the yeast cell cycle.The investigation of the activities of the RNA polymerases (RNA nucleotidyltransferase, EC 2.7.7.6) during the cell cycle of Saccharomyces cerevisiae offers an approach to study the regulation of these enzymes and their relationship with other biochemical events. The synthesis of RNA (1, 2) and of the ribosomal proteins (3) is continuous during the yeast cell cycle, while the replication of the DNA and the synthesis of many enzymes occur in a discontinuous, step-wise fashion (4, 5).The study of the activities of the nuclear RNA polymerases I and II (6) during the yeast cell cycle has been facilitated by the use of a method which allows the separation of cells at different stages of the cell cycle from an exponential culture by means of their centrifugation in a sucrose gradient using a zonal rotor (7). This method leads to a high yield of cells and therefore meaningful determinations of the RNA polymerase activities which otherwise are difficult to obtain with synchronous cultures studied at lower cell densities.The results reported here indicate that the level of the activities of the RNA polymerase I and II follow different patterns during the yeast cell cycle. Consequently, in S. cerevisiae there are independent mechanisms for the regulation of these two enzymes. MATERIAL AND METHODSChemicals. Nucleoside triphosphates, dithiothreitol, phenylmethylsulfonyl fluoride (PAISF), EDTA, and calf-thymus DNA were obtained from Sigma Chemical Co., 2-mercaptoethanol from Eastman Kodak Co., DEAE-Sephadex A25 from Pharmacia, poly(dA-dT) from Biopolymers Inc., and tritium-labeled UTP (26.9 Ci/mmol) from New England Nuclear Corp.High 30 samples and the number and size of the cells in each fraction were analyzed with an electronic cell counter (Coulter Counter model B) and a multi channel particle size analyzer (Coulter Channelyzer) using a 50-,um aperture tube after dilution of the samples to approximately 5 X 104 cells per ml in 0.9% saline. The samples were pooled in a total of 8 fractions containing cells at different stages of the cell cycle. The cells were then quickly centrifuged, washed, and frozen.Solubilization and Separation of the RNA Polynmerases I and II. The cells from the different fractions were suspended in 4 ml of buffer B without glycerol containing 0.5 M ammonium sulfate. The frozen cell suspension was passed through...

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Transcription in Yeast: A Factor that Stimulates Yeast RNA Polymerases

Cited by 28 publications

References 18 publications

Effect of non-histone chromosomal proteins on transcription in vitro in sea-urchin

Effect of non-histone chromosomal proteins on transcription in vitro in sea-urchin

A protein cofactor that stimulates the activity of DNA-dependent RNA polymerase I on double-stranded DNA

Independent Regulation of the Nuclear RNA Polymerases I and II During the Yeast Cell Cycle

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