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 a positive regulatory protein in Escherichia coli: the product of the cysB gene
โ Scribed by Mascarenhas, D. M. ;Yudkin, M. D.
- Publisher
- Springer
- Year
- 1980
- Tongue
- English
- Weight
- 413 KB
- Volume
- 177
- Category
- Article
- ISSN
- 0026-8925
No coin nor oath required. For personal study only.
โฆ Synopsis
From the specialized transducing bacteriophage lambdacysB, recombinant phages lambdacysB242 and lambdacysB257 have been obtained, each of which carries an amber mutation in the cysB cistron. A comparison of polyacrylamide gel electrophoretic profiles of labelled extracts from uv-irradiated bacteria that had been infected with lambdacysB+ or with lambdacysB-amber phages, led to the identification of a 39,000-dalton polypeptide as the product of the cysB gene. The native protein was purified to near radiochemical purity and was found to be an oligomer with an isoelectric point close to pH 7.
๐ SIMILAR VOLUMES
The gene secY (or prlA) is essential for protein export across the cytoplasmic membrane of Escherichia coli. The protein product of secY has been identified using the gene cloned under the control of the pL promoter of phage lambda in combination with the maxicell system. The protein was found to ha
A specialized transducing lambda phage carrying the dnaN and dnaA genes of Escherichia coli specifies two proteins of about 41 and 48 kilodaltons (kd). The temperature-sensitive mutations, dnaN59 and dnaA167, were found to result in altered isoelectric points of the 41 and 48 kd proteins, respective
Eight new deletion mutations in the prn gene cluster involved in L-proline catabolism in Aspergillus nidulans have been characterised and mapped. Three of these are located within prnA, the regulatory gene mediating proline induction, and confirm the positive nature of the action of the prnA product