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  Translationally coupled initiation of protein synthesis in Bacillus subtilis

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.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0000-CF24-F Version Permalink: http://hdl.handle.net/21.11116/0000-0000-CF25-E
Genre: Journal Article

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NuclAcidRes_13_1985_893.pdf (Any fulltext), 2MB
 
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 Creators:
Sprengel, Rolf1, 2, 3, Author              
Reiss, Bernd, Author
Schaller, Heinz, Author
Affiliations:
1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              
2Rolf Sprengel Group, Max Planck Institute for Medical Research, Max Planck Society, ou_1497741              
3Olfaction Web, Max Planck Institute for Medical Research, Max Planck Society, ou_1497733              

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 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.

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Language(s): eng - English
 Dates: 1984-12-191985-01-161985-02-11
 Publication Status: Published in print
 Pages: 17
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 Rev. Type: Peer
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Title: Nucleic Acids Research (London)
  Other : Nucleic Acids Res
Source Genre: Journal
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Publ. Info: Oxford : Oxford University Press
Pages: - Volume / Issue: 13 (3) Sequence Number: - Start / End Page: 893 - 909 Identifier: ISSN: 0305-1048
CoNE: https://pure.mpg.de/cone/journals/resource/110992357379342