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Site-directed, Ligase-Independent Mutagenesis (SLIM): a single-tube methodology approaching 100% efficiency in 4 h.
Site-directed, Ligase-Independent Mutagenesis (SLIM) is a novel PCR-mediated mutagenesis approach that can accommodate all three sequence modification types (insertion, deletion and substitution).Expand
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Evolution of a molecular switch: universal bacterial GTPases regulate ribosome function
The GTPases comprise a protein superfamily of highly conserved molecular switches adapted to many diverse functions. These proteins are found in all domains of life and often perform essential rolesExpand
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Function of the universally conserved bacterial GTPases.
The GTPase superfamily of cellular regulators is well represented in bacteria. A small number are universally conserved over the entire range of bacterial species. Such a pervasive taxonomicExpand
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Site-directed, Ligase-Independent Mutagenesis (SLIM) for highly efficient mutagenesis of plasmids greater than 8kb.
Modifying the Site-directed, Ligase-Independent Mutagenesis (SLIM) protocol from a single reaction mode to a two-reaction mode enables highly efficient mutagenesis of plasmid constructs that exceedExpand
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A GTP-binding protein of Escherichia coli has homology to yeast RAS proteins.
The DNA sequence of a gene (era) located immediately downstream of the gene (rnc) encoding ribonuclease III of Escherichia coli was determined and found to encode a protein of 316 amino acidExpand
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A GTP-binding protein (Era) has an essential role in growth rate and cell cycle control in Escherichia coli.
Era is a membrane-associated GTP-binding protein which is essential for cell growth in Escherichia coli. In order to examine the physiological role of Era, strains in which Era was expressed at 40Expand
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The Escherichia coli Ras-like protein (Era) has GTPase activity and is essential for cell growth.
The era gene of Escherichia coli encodes a protein (Era) which is similar to the eucaryotic RAS family of proteins. We report here that purified Era possesses both GTP-binding and GTPase activities.Expand
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In vivo selection of conditional-lethal mutations in the gene encoding elongation factor G of Escherichia coli.
The ribosome translocation step that occurs during protein synthesis is a highly conserved, essential activity of all cells. The precise movement of one codon that occurs following peptide bondExpand
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Initiation factor IF2, thiostrepton and micrococcin prevent the binding of elongation factor G to the Escherichia coli ribosome.
The bacterial translational GTPases (initiation factor IF2, elongation factors EF-G and EF-Tu and release factor RF3) are involved in all stages of translation, and evidence indicates that they bindExpand
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Cross-species complementation of the indispensable Escherichia coli era gene highlights amino acid regions essential for activity.
Era is an essential GTP binding protein in Escherichia coli. Two homologs of this protein, Sgp from Streptococcus mutans and Era from Coxiella burnetii, can substitute for the essential function ofExpand
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