Journal ArticleDOI
Barriers to the heterospecific gene expression among prokaryotes
S.D. Ehrlich,V. Sgaramella +1 more
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Nine genes active in Bacillus subtilis are also expressed in Escherichia coli, but none of the five E. coli genes tested so far function in B. subtILis.About:
This article is published in Trends in Biochemical Sciences.The article was published on 1978-10-01. It has received 23 citations till now. The article focuses on the topics: Bacillus subtilis & Gene.read more
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Gene expression in Streptomyces : Construction and application of promoter-probe plasmid vectors in Streptomyces lividans
Mervyn J. Bibb,Stanley N. Cohen +1 more
TL;DR: Promoter-probe plasmid vectors constructed for Streptomyces lividans using expression of the Escherichia coli chloramphenicol acetyltransferase gene as an indicator of promoter activity indicate that genus or species-specific factors may present barriers to the expression of bacterial genetic material in certain heterologous cellular environments.
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Microbiological and Biotechnological Aspects of Metabolism of Carbamates and Organophosphates
S Chapalamadugu,G R Chaudhry +1 more
TL;DR: In this review, recent advances in the biochemical and genetic aspects of microbial degradation of carbamate and organophosphate compounds are discussed and areas in need of further investigation identified.
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Nucleotide sequences encoding and promoting expression of three antibiotic resistance genes indigenous to Streptomyces.
TL;DR: An extremely biased codon usage pattern that reflects the high G+C composition of Streptomyces DNA was observed for the protein-coding regions of the tsr and vph genes, and of the previously sequenced aph gene.
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Cloning and expression in streptomyces lividans of antibiotic resistance genes derived from Escherichia coli.
TL;DR: Findings make it unlikely that the biologically active CM acetyltransferase was being made in S. lividans as part of a fused protein, but indicate that the ATG start codon used for initiation of translation of the Cm resistance gene in E. coli was also utilized in S.'s lividan host.
References
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Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma.
TL;DR: In this article, it was shown that in vitro completion of these nascent light chains resulted in the synthesis of some chains having the same mol wt as the authentic secreted light chain, because of completion of in vivo proteolytically processed chains and of other chains which, due to the completion of unprocessed chains, have the same moll wt, as the precursor of the light chain.
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Expression in Escherichia coli of a Chemically Synthesized Gene for the Hormone Somatostatin
Keiichi Itakura,Tadaaki Hirose,Roberto Crea,Arthur D. Riggs,Herbert L. Heyneker,Francisco Bolívar,Herbert W. Boyer +6 more
TL;DR: This work has reported the first synthesis of a functional polypeptide product from a gene of chemically synthesized origin, including the sequence of amino acids corresponding to somatostatin, in vitro.
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Ovalbumin gene is split in chicken DNA
TL;DR: The ovalbumin gene is split in chicken DNA and two interruptions in the sequences coding for ovalbumIn mRNA have been detected, at least one of them lying in the protein coding sequence.
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Subunit I of Qβ Replicase and 30 S Ribosomal Protein Sl of Escherichia coli EVIDENCE FOR THE IDENTITY OF THE TWO PROTEINS
Albert J. Wahba,Martha J. Miller,Alain Niveleau,Terry A. Landers,Gordon G. Carmichael,Klaus Weber,David A. Hawley,Lawrence I. Slobin +7 more
TL;DR: Subunit I of the RNA phage-specific Qβ replicase is shown to be identical with the Escherichia coli 30 S ribosomal protein Sl by the following criteria: ability to restore Qβ RNA-directed activity of Qβ Replicase lacking subunit I, immunological cross-reactivity, and identity of the first four amino acids at the NH2 terminus.
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In vivo degradation of nonsense fragments in E. coli.
TL;DR: Nonsense fragments produced by amber and ochre mutants of the z gene of E. coli are rapidly degraded during exponential growth, while wild type β-galactosidase is stable in the same conditions.