Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.7.6 (RNA polymerase)
 34,946 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The structural gene for elongation factor EF-TS (tsf) and that for ribosomal protein S2 (rpsB) have been identified in E. coli. Both genes are carried by lambda transducing phages that have been isolated as dapD+polC+ transducing phages. Synthesis of both S2 and EF-Ts was demonstrated in ultraviolet light-irradiated E. coli cells infected with these phages. Experiments were also done using other transducing phages that carry dapD+ but not polC+. The data indicate that both the tsf and rpsB genes map near dapD at about 4 min on the E. coli genetic map. This location is different from the two chromosomal locations, the str-spc region and the rif region, where many ribosomal protein genes, the genes for RNA polymerase components, as well as other elongation factor genes (fus, tufA, and tufB) are located.
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PMID:Identification of genes for elongation factor Ts and ribosomal protein S2 in E. coli. 78 23

A specialized transducing bacteriophage lambdadpolCdap D-9 has been isolated that carries the structural gene for EF-Ts1 (tsf). The presence of EF-Ts among the proteins synthesized under the direction of this phage in UVL-inactivated cells has been detected by two-dimensional gel electrophoresis and has been verified by antibody precipitation. In an induced lysogen of this phage the relative rate of synthesis of EF-Ts is increased 4-fold. Evidence is presented which suggest that the structural genes for ribosomal protein S2 (rpsB) and RNA polymerase sigma factor (sit) also lies on lambdadpolCdap D-9.
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PMID:A transducing bacteriophage lambda carrying the structural gene for elongation factor Ts. 79 84

Antisera against a synthetic tetradecameric peptide with the sequence DLIQEGNIGLMKAV, which is present in region 2.2 of both sigma 70 and sigma 32 subunits of Escherichia coli RNA polymerase, cross-reacted with more than 10 E. coli proteins including these two sigma subunits. Four major species of these cross-reacting proteins (SCRPs) were purified. N-Terminal amino acid sequence analysis revealed that one of them (SCRP-27A) was an as yet unidentified protein while the other three (SCRP-34, SCRP-27B and SCRP-23) were thioredoxin reductase, ribosomal protein S2, and alkyl hydroperoxide reductase, respectively. Immunological competition experiments with various fragments of this sigma region 2.2 peptide indicated that the anti-sigma peptide serum contained at least three different species of antibodies. All the four SCRPs analyzed here reacted with an antibody against a C-terminus-proximal epitope.
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PMID:Identification of Escherichia coli proteins cross-reacting with antibodies against region 2.2 peptide of RNA polymerase sigma subunit. 157 37

The DNA-dependent RNA polymerases from heat-shocked and vegetatively grown cells of Bacillus subtilis were isolated and compared. The RNA polymerase from non-stressed cells had the well known alpha, beta, beta' and sigma composition of eubacterial RNA polymerases. The RNA polymerase from heat-shocked cells exhibited one additional band shown by SDS-PAGE. N-terminal sequencing of the first 16 amino acids of the associated protein demonstrated its identity with the ribosomal protein S2.
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PMID:Copurification of ribosomal protein S2 and DNA-dependent RNA polymerase from heat-shocked cells of Bacillus subtilis. 909 Jan 22