Lysis gene of bacteriophage MS2 is activated by translation termination at the overlapping coat gene.

[1]  B. Berkhout,et al.  Determination of the RNA secondary structure that regulates lysis gene expression in bacteriophage MS2. , 1987, Journal of molecular biology.

[2]  D. Peabody,et al.  Effect of upstream reading frames on translation efficiency in simian virus 40 recombinants , 1986, Molecular and cellular biology.

[3]  D. Peabody,et al.  Termination-reinitiation occurs in the translation of mammalian cell mRNAs , 1986, Molecular and cellular biology.

[4]  A. Jacobson,et al.  The complete nucleotide sequence of the group II RNA coliphage GA. , 1986, Journal of biochemistry.

[5]  K. Cone,et al.  Functional analysis of lac repressor restart sites in translational initiation and reinitiation. , 1985, Journal of molecular biology.

[6]  K. Cone,et al.  Messenger RNA conformation and ribosome selection of translational reinitiation sites in the lac repressor mRNA. , 1985, Journal of molecular biology.

[7]  D. Dubnau,et al.  Evidence for the translational attenuation model: ribosome-binding studies and structural analysis with an in vitro run-off transcript of ermC. , 1985, Nucleic acids research.

[8]  M. Mayford,et al.  Messenger RNA from Staphylococcus aureus that specifies macrolide-lincosamide-streptogramin resistance. Demonstration of its conformations and of the leader peptide it encodes. , 1985, Journal of molecular biology.

[9]  B. Berkhout,et al.  Mechanism of translational coupling between coat protein and replicase genes of RNA bacteriophage MS2. , 1985, Nucleic acids research.

[10]  K. Jensen,et al.  Codon-defined ribosomal pausing in Escherichia coli detected by using the pyrE attenuator to probe the coupling between transcription and translation. , 1985, Nucleic acids research.

[11]  B. Berkhout,et al.  Translational interference at overlapping reading frames in prokaryotic messenger RNA. , 1985, Gene.

[12]  R. Lloubès,et al.  Translation is a non-uniform process. Effect of tRNA availability on the rate of elongation of nascent polypeptide chains. , 1984, Journal of molecular biology.

[13]  S. Pedersen.  Escherichia coli ribosomes translate in vivo with variable rate. , 1984, The EMBO journal.

[14]  G Humphreys,et al.  Codon usage can affect efficiency of translation of genes in Escherichia coli. , 1984, Nucleic acids research.

[15]  C. Yanofsky,et al.  A ribosome binding site sequence is necessary for efficient expression of the distal gene of a translationally-coupled gene pair. , 1984, Nucleic acids research.

[16]  M. Kozak,et al.  Selection of initiation sites by eucaryotic ribosomes: effect of inserting AUG triplets upstream from the coding sequence for preproinsulin. , 1984, Nucleic acids research.

[17]  C. Squires,et al.  Translational coupling of the trpB and trpA genes in the Escherichia coli tryptophan operon , 1984, Journal of bacteriology.

[18]  B. Berkhout,et al.  Opening the closed ribosome-binding site of the lysis cistron of bacteriophage MS2 , 1983, Nature.

[19]  J. Langowski,et al.  Does the specific recognition of DNA by the restriction endonuclease EcoRI involve a linear diffusion step? Investigation of the processivity of the EcoRI endonuclease. , 1983, Nucleic acids research.

[20]  C Yanofsky,et al.  Attenuation in amino acid biosynthetic operons. , 1982, Annual review of genetics.

[21]  M. Gouy,et al.  Codon usage in bacteria: correlation with gene expressivity. , 1982, Nucleic acids research.

[22]  D. Schümperli,et al.  Translational coupling at an intercistronic boundary of the Escherichia coli galactose operon , 1982, Cell.

[23]  T. Ikemura.  Correlation between the abundance of yeast transfer RNAs and the occurrence of the respective codons in protein genes. Differences in synonymous codon choice patterns of yeast and Escherichia coli with reference to the abundance of isoaccepting transfer RNAs. , 1982, Journal of molecular biology.

[24]  W. Fiers,et al.  Preferential codon usage in prokaryotic genes: the optimal codon-anticodon interaction energy and the selective codon usage in efficiently expressed genes. , 1982, Gene.

[25]  W. Fiers,et al.  Lysis gene expression of RNA phage MS2 depends on a frameshift during translation of the overlapping coat protein gene , 1982, Nature.

[26]  P. V. von Hippel,et al.  Diffusion-driven mechanisms of protein translocation on nucleic acids. 3. The Escherichia coli lac repressor--operator interaction: kinetic measurements and conclusions. , 1981, Biochemistry.

[27]  W. Fiers,et al.  Plasmid vectors for high-efficiency expression controlled by the PL promoter of coliphage lambda. , 1981, Gene.

[28]  L. Gold,et al.  Translational reinitiation in the rIIB cistron of bacteriophage T4. , 1981, Journal of molecular biology.

[29]  M. Nomura,et al.  Feedback regulation of ribosomal protein synthesis in E. coli: Localization of the mRNA target sites for repressor action of ribosomal protein L1 , 1981, Cell.

[30]  M. D. Rosa.  Structure analysis of three T7 late mRNA ribosome binding sites. , 1981, Journal of molecular biology.

[31]  T. Ikemura.  Correlation between the abundance of Escherichia coli transfer RNAs and the occurrence of the respective codons in its protein genes. , 1981, Journal of molecular biology.

[32]  C. Yanofsky,et al.  Translational coupling during expression of the tryptophan operon of Escherichia coli. , 1980, Genetics.

[33]  T. Blumenthal,et al.  Overlapping genes in rna phage: a new protein implicated in lysis , 1979, Cell.

[34]  A. Morris,et al.  Nonuniform size distribution of nascent peptides. The effect of messenger RNA structure upon the rate of translation. , 1979, Archives of biochemistry and biophysics.

[35]  Fred Russell Kramer,et al.  Template-determined, variable rate of RNA chain elongation , 1978, Cell.

[36]  W. Fiers,et al.  Nucleotide Sequence of the Gene Coding for the Bacteriophage MS2 Coat Protein , 1972, Nature.

[37]  R. E. Webster,et al.  Fate of the message-ribosome complex upon translation of termination signals. , 1969, Journal of molecular biology.

[38]  N. Zinder,et al.  Cell Lysis: Another Function of the Coat Protein of the Bacteriophage f2 , 1968, Science.