BIOMAT Database Logo BIOMAT Database Logo

Conversion of Bacillus subtilis RNA polymerase activity in vitro by a protein induced by phage SP01. 1975

J J Duffy, and R L Petrusek, and E P Geiduschek

A protein fraction from B. subtilis infected with phage SP01 (fraction LGG) stimulates the activity of RNA polymerase (EC 2.7.7.6; nucleosidetriphosphate:RNA nucleotidyltransferase) core from uninfected bacteria. Fraction LGG contains a protein (P-28, molecular weight 28,000) that is labeled after phage infection and binds tightly to RNA polymerase core at a relatively high ionic strength. B. subtilis RNA polymerase core with bound P-28 has the transcription specificity of the previously purified, phage-modified B-P RNA polymerase; the latter contains two subunits, v-28 and v-13 (molecular weights 28,000 and 13,000, respectively) that are synthesized after phage infection. Both enzymes transcribe SP01 DNA preferentially and direct the asymmetric synthesis of viral middle RNA. P-28, like v-28, binds more tightly to B. subtilis RNA polymerase core than the B. subtilis initiation factor, sigma, at higher ionic strength. We propose that P-28 and v-28 are the same protein. P-28 and, by implication, v-28 suffice to endow the bacterial RNA polymerase core with a novel transcription specificity.

UI MeSH Term Description Entries
D007930 Leucine An essential branched-chain amino acid important for hemoglobin formation. L-Leucine,Leucine, L-Isomer,L-Isomer Leucine,Leucine, L Isomer
D009693 Nucleic Acid Hybridization Widely used technique which exploits the ability of complementary sequences in single-stranded DNAs or RNAs to pair with each other to form a double helix. Hybridization can take place between two complimentary DNA sequences, between a single-stranded DNA and a complementary RNA, or between two RNA sequences. The technique is used to detect and isolate specific sequences, measure homology, or define other characteristics of one or both strands. (Kendrew, Encyclopedia of Molecular Biology, 1994, p503) Genomic Hybridization,Acid Hybridization, Nucleic,Acid Hybridizations, Nucleic,Genomic Hybridizations,Hybridization, Genomic,Hybridization, Nucleic Acid,Hybridizations, Genomic,Hybridizations, Nucleic Acid,Nucleic Acid Hybridizations
D011232 Chemical Precipitation The formation of a solid in a solution as a result of a chemical reaction or the aggregation of soluble substances into complexes large enough to fall out of solution. Precipitation, Chemical
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D002499 Centrifugation, Density Gradient Separation of particles according to density by employing a gradient of varying densities. At equilibrium each particle settles in the gradient at a point equal to its density. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Centrifugations, Density Gradient,Density Gradient Centrifugation,Density Gradient Centrifugations,Gradient Centrifugation, Density,Gradient Centrifugations, Density
D002846 Chromatography, Affinity A chromatographic technique that utilizes the ability of biological molecules, often ANTIBODIES, to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Chromatography, Bioaffinity,Immunochromatography,Affinity Chromatography,Bioaffinity Chromatography
D002848 Chromatography, DEAE-Cellulose A type of ion exchange chromatography using diethylaminoethyl cellulose (DEAE-CELLULOSE) as a positively charged resin. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) DEAE-Cellulose Chromatography,Chromatography, DEAE Cellulose,DEAE Cellulose Chromatography
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D000645 Ammonium Sulfate Sulfuric acid diammonium salt. It is used in CHEMICAL FRACTIONATION of proteins. Sulfate, Ammonium
D001412 Bacillus subtilis A species of gram-positive bacteria that is a common soil and water saprophyte. Natto Bacteria,Bacillus subtilis (natto),Bacillus subtilis subsp. natto,Bacillus subtilis var. natto

Related Publications

J J Duffy, and R L Petrusek, and E P Geiduschek
RNA polymerase from phage SP01-infected and uninfected Bacillus subtilis.
June 1975, The Journal of biological chemistry,
J J Duffy, and R L Petrusek, and E P Geiduschek
Synthesis of specific functional messenger RNA in vitro by phage-SP01-modified RNA polymerase of Bacillus subtilis.
December 1975, Proceedings of the National Academy of Sciences of the United States of America,
J J Duffy, and R L Petrusek, and E P Geiduschek
Transcription of cloned DNA from Bacillus subtilis phage SP01. Requirement for hydroxymethyluracil-containing DNA by phage-modified RNA polymerase.
May 1980, Journal of molecular biology,
J J Duffy, and R L Petrusek, and E P Geiduschek
Ribonucleoside triphosphate concentration-dependent termination of bacteriophage SP01 transcription in vitro by Bacillus subtilis RNA polymerase.
June 1984, Virology,
J J Duffy, and R L Petrusek, and E P Geiduschek
Promoter recognition by phage SP01-modified RNA polymerase.
March 1978, Proceedings of the National Academy of Sciences of the United States of America,
J J Duffy, and R L Petrusek, and E P Geiduschek
Highly asymmetric transcription by RNA polymerase containing phage-SP01-induced polypeptides and a new host protein.
April 1975, Proceedings of the National Academy of Sciences of the United States of America,
J J Duffy, and R L Petrusek, and E P Geiduschek
New phage-SPO1-induced polypeptides associated with Bacillus subtilis RNA polymerase.
July 1974, Proceedings of the National Academy of Sciences of the United States of America,
J J Duffy, and R L Petrusek, and E P Geiduschek
In vitro synthesis of ribosomal RNA by Bacillus subtilis RNA polymerase.
February 1972, Proceedings of the National Academy of Sciences of the United States of America,
J J Duffy, and R L Petrusek, and E P Geiduschek
A novel DNA polymerase induced by Bacillus subtilis phage phi 29.
December 1983, Nucleic acids research,
J J Duffy, and R L Petrusek, and E P Geiduschek
New RNA polymerase from Bacillus subtilis infected with phage PBS2.
November 1974, Nature,
Copied contents to your clipboard!