J.M. Dubert

Université Paris Cité

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G Lagrue

Hôpital Albert-Chenevier

Guy Rostoker

Générale de Santé

M. Petit-Phar

Inserm

Brigitte Hermier

Institut Jacques Monod

Philippe Lang

Interfaces Traitements Organisation et Dynamique des Systèmes

B Weil

Hôpitaux Universitaires Henri-Mondor

Luisa Hirschbein

Centre National pour la Recherche Scientifique et Technique (CNRST)

A Paraf

Hôpital Avicenne

François Nau

Université de Poitiers

M.A. Pech

Inserm

Cooperative Institutions

Inserm

Centre National de la Recherche Scientifique

Université Paris Cité

Pediatric Nephrology of Alabama

Institut Pasteur

Service de la Santé Publique

Hospital Clínic de Barcelona

Centre Hospitalier Universitaire Henri-Mondor

King Chulalongkorn Memorial Hospital

Universitat de Barcelona

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Structural and enzymatic properties of the E. coli RNA polymerase subunits

FEBS Letters (1969)

Luisa Hirschbein J.M. Dubert Ch. Babinet

10.1016/0014-5793(69)80152-3

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Citations (3)

[On the nature of the secondary response].

PubMed (1956)

J.M. Dubert

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Citations (1)

Differences de specificite entre les methylases de myelome et de foie vis‐a‐vis du tRNA d'E. coli K 12

FEBS Letters (1969)

François Nau Guy Pétrissant J.M. Dubert

This paper describes an attempt to find a difference between the patterns of methylation of E. coli tRNA by extracts of two mouse tissues. Two samples of tRNAs, methylated in two separate experiments with extracts of myeloma and of liver in presence of either 14 C or 3 H S‐Adenosyl‐L‐Methionine, were pooled and fractionated together on a RPC column. The results show a difference in the specificities of the two extracts. Chromatography on DEAE Sephadex suggests that the tRNA Met is methylated by the enzymes on the myeloma, while enzymes from liver react very little, if at all, with that particular tRNA species. Studies have been undertaken in order to find out whether similar differences can also be demonstrated in homologous systems.

Sephadex

10.1016/0014-5793(69)80273-5

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Citations (5)

Action of Protease I of Escherichia coli on RNA Polymerase of Same Origin

European Journal of Biochemistry (1973)

Brigitte Hermier Michèle Pacaud J.M. Dubert

The recently isolated protease I of Escherichia coli leads to the partial degradation of RNA polymerase of E. coli and causes, in particular, the splitting of subunits ββ′ into fragments of approximately the same size as that of factor σ. This action is similar to that of papaïn or α‐chymotrypsin employed for short periods at much lower concentrations. The immunochemical study presented leads to the identification of the origin of the fragments obtained by limited proteolysis and shown the lack of cross reaction between subunits ββ′ and σ factor.

Proteolysis

10.1111/j.1432-1033.1973.tb03063.x

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Affinité différentielle de la RNA polymérase pour divers polyribonucléotides synthétiques

European Journal of Biochemistry (1967)

Luisa Hirschbein J.M. Dubert C. Babinet

Using synthetic polyribonucleotides templates as models, the problems of attachment or detachment of DNA dependent‐RNA polymerase to its template have been investigated. In addition, the hypothesis that sites of initiation or termination of transcription might be determined by some specific base sequences was tested with these models. In order to allow a distinction between the transcription process and its first step, which is the binding of the enzyme to its template, the inhibition by different polyribonucletides of the transcription of DNA was examined. A wide range of relative effects was found (Fig. 3). It is remarkable that the polyribonucleotides Poly G and Poly I showing the highest affinities for the enzyme, as well as the homopolymer pair Poly (G + C) of low affinity could not be transcribed into their complementary sequences when used as template. When using the polyribonucleotides as template instead of DNA, the K m for triphosphate binding is about 30 fold higher. It was shwon in inhibition experiments that for a given system, a polyribonucleotide was more efficient as an inhibitor as the concentration of its complementary triphosphate was increased (Fig. 4): this result shows that the triphosphate contributes to the stability of the polyribonucleotide‐enzyme complex. The properties of Poly I or Poly G of having very high affinity for RNA polymerase and of not being transcribed could be used to trap the enzyme not bound to its template at any time before or during the transcription process. Preliminary results are reported in Fig.5. The fact that Poly (G + C) has barely detectable affinity for RNA polymerase can explain the kinetic results obtained when Poly C is used as a template; the G/C ratio reaches one at the end of the reaction and no further incorporation of GMP is observed when enzyme or GTP is added. Only the addition of Poly C can allow resumption of incorporation of the complementary nucleotides (Fig.2A). Consistent with these results is the observation that the enzyme and the product of the reaction migrate separately in a sucrose gradient centrifugation. Our studies show that the relative affinity of RNA polymerase for different homopolymer pairs Poly (A + U), Poly (G + C) is dependent on the nature of the bases involved in these ordered double helical structures.

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10.1111/j.1432-1033.1967.tb00054.x

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Citations (33)

[New method of separation of blood proteins by methanol; application to horse and rabbit blood].

PubMed (1953)

J.M. Dubert P Slizewicz P Rebeyrotte M Macheboeuf

Rabbit (cipher)

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Citations (9)

Inhibition of murine plasmacytoma TEPC 15 by its specific antigen

Nature (1975)

A Paraf Claudine Guérin-Marchand Jacques Aubry J.M. Dubert

Myeloma protein

10.1038/255488a0

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Citations (17)

Regulation of Metabolic Breakdown and Synthesis of Messenger RNA in Bacteria

Cold Spring Harbor Symposia on Quantitative Biology (1963)

F Gros J.M. Dubert A. Tissières Suzanne Bourgeois M.J. Michelson

Since the discovery of rapidly turning over RNA fractions in bacteria (Nomura, Hall, and Spiegelman, 1960; Brenner, Jacob, and Meselson, 1961; Gros, Gilbert, Hiatt, Kurland, Risebrough, and Watson, 1961) as well as in other organisms (Cheng, 1961; Hiatt, 1962; Sibatani, de Kloet, Allfrey, and Mirsky, 1962; Scherrer and Darnell, 1962) very extensive studies have been devoted to their molecular characteristics, their composition, (Gros et al., 1961; Spiegelman, 1961) and their physico-chemical properties (Bautz, 1963). These studies have led to the conclusion that a large part of rapidly labeled RNA chains represent the sum of the transcription products of the genetic material the “structural messengers” (M-RNA), the remainder corresponding to metabolic precursors of the ribosomal or transfer RNA (Bolton and McCarthy, 1962).

Transcription

10.1101/sqb.1963.028.01.045

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Citations (42)

In vitro differentiation of a mouse plasmocytoma: its phenothypically stabilized states

Immunochemistry (1970)

A Paraf M. A. Moyne J F Duplan R. Scherrer M Stanislawski

10.1016/0019-2791(70)90101-1

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Author Index, Vol. 59, 1991

The Nephron journals/Nephron journals (1991)

Nigel Wardle Peter Pietschmann Andreas Vychytil W. Woloszczuk Josef Kovařík

10.1159/000186685

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