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A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes.
A nomenclature is described for restriction endonucleases, DNA methyltransferases, homing endonucleases and related genes and gene products. It provides explicit categories for the many differentExpand
Homing endonucleases: keeping the house in order.
The evolution of homing endonucleases is considered, both at the structure-function level and in terms of their persistence in widely divergent biological systems. Expand
Escherichia coli protein analogs StpA and H‐NS: regulatory loops, similar and disparate effects on nucleic acid dynamics.
It is proposed that in addition to its role as a molecular back‐up of H‐NS, StpA's superior effect on RNA may be exploited under some specific cellular conditions to promote differential gene expression. Expand
Introns as mobile genetic elements.
Riboregulation in Escherichia coli: DsrA RNA acts by RNA:RNA interactions at multiple loci.
It is demonstrated that DsrA acts via specific RNA:RNA base pairing interactions at the hns locus to antagonize H-NS translation and suggested that positive regulation of rpoS by D srA occurs by formation of an RNA structure that activates a cis-acting translational operator. Expand
A trans-acting RNA as a control switch in Escherichia coli: DsrA modulates function by forming alternative structures.
  • R. Lease, M. Belfort
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences…
  • 29 August 2000
It is shown that DsrA enhances hns mRNA turnover yet stabilizes rpoS mRNA, either directly or via effects on translation, which leads to opposite regulatory consequences for target RNAs. Expand
Group I and group II introns
This review summarizes current information about the structures of group I and group II introns, their RNA‐catalyzed reactions, the facilitation of RNA‐Catalyzed splicing by protein factors, and the ability of the introns to function as mobile elements. Expand
Configuration of the catalytic GIY-YIG domain of intron endonuclease I-TevI: coincidence of computational and molecular findings.
The N-terminal catalytic domain corresponds precisely to the GIY-YIG module defined by sequence comparisons of 57 proteins including more than 30 newly reported members of the family, raising the possibility that this region may adopt an alternate conformation upon DNA binding. Expand
Catalytic domain structure and hypothesis for function of GIY-YIG intron endonuclease I-TevI
The crystal structure of the catalytic domain of I-TevI, the first of any GIY-YIG endonuclease, reveals a novel α/β-fold with a central three-stranded antiparallel β-sheet flanked by three helices, suggesting the possibility of mechanistic relationships among these different families of homing endonucleases despite completely different folds. Expand
A bacterial group II intron encoding reverse transcriptase, maturase, and DNA endonuclease activities: biochemical demonstration of maturase activity and insertion of new genetic information within
It is shown that the Lactococcal intron can be expressed and spliced efficiently in Escherichia coli, and the specificity of the endonuclease and reverse splicing reactions can be changed predictably by modifying the RNA component. Expand