Unique features in the ribosome binding site sequence of the gram-positive Staphylococcus aureus beta-lactamase gene.

McLaughlin, Jane R.; Murray, C L; Rabinowitz, Jesse C.

doi:10.1016/s0021-9258(19)68589-3

Cited by 476 publications

(21 citation statements)

References 48 publications

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“…It has a high degree of complementarity to the B. subtilis 16S RNA and good spacing from the initiation site. This conforms well with a previous observation that genes from Gram positive bacteria initiating with a TTG codon often contain strong Shine Dalgarno complementarity (56).…”

Section: Characterization Of Mbamhi Modificationsupporting

confidence: 93%

Characterization of the cloned BamHI restriction modification system: its nucleotide sequence, properties of the methylase, and expression in heterologous hosts

et al. 1991

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The BamHI restriction modification system was previously cloned into E. coli and maintained with an extra copy of the methylase gene on a high copy vector (Brooks et al., (1989) Nucl. Acids Res. 17, 979-997). The nucleotide sequence of a 3014 bp region containing the endonuclease (R) and methylase (M) genes has now been determined. The sequence predicts a methylase protein of 423 amino acids, Mr 49,527, and an endonuclease protein of 213 amino acids, Mr 24,570. Between the two genes is a small open reading frame capable of encoding a 102 amino acid protein, Mr 13,351. The M. BamHI enzyme has been purified from a high expression clone, its amino terminal sequence determined, and the nature of its substrate modification studied. The BamHI methylase modifies the internal C within its recognition sequence at the N4 position. Comparisons of the deduced amino acid sequence of M. BamHI have been made with those available for other DNA methylases: among them, several contain five distinct regions, 12 to 22 amino acids in length, of pronounced sequence similarity. Finally, stability and expression of the BamHI system in both E. coli and B. subtilis have been studied. The results suggest R and M expression are carefully regulated in a 'natural' host like B. subtilis.

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Section: Characterization Of Mbamhi Modificationsupporting

confidence: 93%

Characterization of the cloned BamHI restriction modification system: its nucleotide sequence, properties of the methylase, and expression in heterologous hosts

et al. 1991

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“…-90.44 kJ). This is similar to Shine-Dalgarno regions seen for other genes from gram-positive organisms (26,29,30). Immediately following the end of the coding sequence is a potential hairpin structure, with a stem of 11 terminators; however, functional evidence for any such role is still lacking (42,46,47).…”

Section: Discussionsupporting

confidence: 58%

Cloning of the neutral protease gene of Bacillus subtilis and the use of the cloned gene to create an in vitro-derived deletion mutation

Yang¹,

Ferrari²,

Henner³

1984

J Bacteriol

254

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The neutral protease gene of Bacillus subtilis has been cloned, and its nucleotide sequence has been determined. The cloned gene was used to create an in vitro-derived deletion mutation, which was used to replace the wild-type copy of the gene. This deletion, in combination with a deletion of the alkaline protease gene, completely abolished protease production. The loss of the proteases had no detectable effect on growth, morphology, or sporulation.

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“…40). Gram positives are characterized by strong ribosomal binding sites (41) thus we think that GTG168 is the real translational start codon of the Sau96I methyltransferase gene. The reading frame between GTG168 and TGA1458 determines a protein of 430 amino acids (Mr: 49,252).…”

Section: Dna Sequencementioning

confidence: 97%

Cloning and nucleotide sequence of the genes coding for theSau961 restriction and modification enzymes

1990

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The genes coding for the GGNCC specific Sau96I restriction and modification enzymes were cloned and expressed in E. coli. The DNA sequence predicts a 430 amino acid protein (Mr: 49,252) for the methyltransferase and a 261 amino acid protein (Mr: 30,486) for the endonuclease. No protein sequence similarity was detected between the Sau96I methyltransferase and endonuclease. The methyltransferase contains the sequence elements characteristic for m5C-methyltransferases. In addition to this, M.Sau96I shows similarity, also in the variable region, with one m5C-methyltransferase (M.SinI) which has closely related recognition specificity (GGA/TCC). M.Sau96I methylates the internal cytosine within the GGNCC recognition sequence. The Sau96I endonuclease appears to act as a monomer.

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Unique features in the ribosome binding site sequence of the gram-positive Staphylococcus aureus beta-lactamase gene.

Cited by 476 publications

References 48 publications

Characterization of the cloned BamHI restriction modification system: its nucleotide sequence, properties of the methylase, and expression in heterologous hosts

Characterization of the cloned BamHI restriction modification system: its nucleotide sequence, properties of the methylase, and expression in heterologous hosts

Cloning of the neutral protease gene of Bacillus subtilis and the use of the cloned gene to create an in vitro-derived deletion mutation

Cloning and nucleotide sequence of the genes coding for theSau961 restriction and modification enzymes

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