English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Translationally coupled initiation of protein synthesis in Bacillus subtilis

MPS-Authors
/persons/resource/persons95439

Sprengel,  Rolf
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;
Rolf Sprengel Group, Max Planck Institute for Medical Research, Max Planck Society;
Olfaction Web, Max Planck Institute for Medical Research, Max Planck Society;

Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Sprengel, R., Reiss, B., & Schaller, H. (1985). Translationally coupled initiation of protein synthesis in Bacillus subtilis. Nucleic Acids Research (London), 13(3), 893-909. doi:10.1093/nar/13.3.893.


Cite as: http://hdl.handle.net/21.11116/0000-0000-CF24-F
Abstract
The neomycin phosphotransferase gene (neo) from Transposon Tn5 is active in Gram-negative bacteria but silent in B. subtilis since it lacks an appropriate ribosome binding site for Gram-positive bacteria. Neo translation could be reactivated by coupling its initiation to the translational termination of the highly expressed beta-lactamase gene (penP) from B. licheniformis. This initiation occurred at the authentic neo start codon. Its efficiency was independent of the nucleotide sequence 5 to the neo gene, but strongly affected by the distance between the termination and initiation codon. It was the highest if both codons overlapped in the sequence ATGA. In B. licheniformis, a translationally coupled neo gene was inducible expressed as the penP gene demonstrating the potential of the technique to monitor the activity of expression units for which no direct assays exists.