Escherichia coli nusB mutants fail to support the activity of a phage lambda gene product, pN, which regulates phage gene expression by influencing transcription termination. We report the identification of the nusB protein on SDS-polyacrylamide gels as a 14,500 dalton protein.
Identification of the E. coli groNB(nusB) gene product
โ Scribed by Swindle, John ;Ajioka, Janet ;Georgopoulos, Costa
- Publisher
- Springer
- Year
- 1981
- Tongue
- English
- Weight
- 545 KB
- Volume
- 182
- Category
- Article
- ISSN
- 0026-8925
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โฆ Synopsis
The E. coli groNB(nusB) gene product has been previously shown to be necessary for bacteriophage lambda N protein function. The product of the groNB gene has been identified on SDS polyacrylamide gels after infection of UV-irradiated E. coli cells with various lambda groNB+ transducing phage derivatives. It is a polypeptide with an apparent molecular weight of 14,000 daltons. Transducing phage carrying either a deletion or an amber mutation in the groNB gene fail to synthesize the 14,000-Mr polypeptide chain upon infection of a sup+ host. However, am+ revertants of the lambda groNBam phage do induce the synthesis of the polypeptide.
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Escherichia coli mutants, called groNB, which block the growth of bacteriophage lambda at the level of action of the gene N product, have been isolated as survivors at 42 degrees C of bacteria carrying a) the defective prophage lambda bio11 i lambda cI857 delta H1 or b) the pcR1 plasmid containing t
We have previously shown that a mutation (groPC259) in the E. coli dnaJ gene renders the cell inviable at high temperatures and arrests bacteriophage lambda DNA replication at all temperatures (Sunshine et al., 1977). We have isolated lambda dnaJ+ transducing phages both by in vitro cloning and by a
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