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The sigma subunit of bacterial RNA polymerase, classically known as an initiation factor, can also operate as an elongation factor with effects that vary with growth phase.

Cryo-EM structures of the eukaryotic clamp loader illustrate the large conformational changes that the clamp loader ATPase undergoes to open the circular sliding clamp and place it onto primer–template DNA.

SCCmec genomic islands encode a novel primase-helicase pair in which priming ability is conferred upon an A-family DNA polymerase domain by a novel protein cofactor.

The crystal structure of Thermus transcription activation complexes containing the transcriptional activator CarD reveals a new mechanism for the activation of transcription.

An inorganic tin oxochloride cluster specifically binds to an intrinsically disordered, histidine-rich, low complexity protein region and arrests de novo transcription initiation without affecting reinitiation.

The primer extension and 5' flap processing activities of DNA polymerase I are physically coordinated by combined movements of the DNA substrate and the 5' nuclease domain of the enzyme.

Fluorescence resonance energy transfer has been used to explore the interactions between DNA polymerases, sliding clamps and clamp loaders as DNA is replicated in human cells.

An evolutionarily conserved protein sequence present in diverse species like yeast, frogs, chickens, and humans binds a well-known template for microtubule nucleation, the gamma-tubulin ring complex, activating and enhancing its ability to nucleate microtubules, even under low tubulin concentrations.

The roles of key telomerase active site residues were elucidated to determine how telomerase selects the correct from the incorrect nucleotide to maintain telomere integrity.

Seven distinct cryo-electron microscopy structures delineate the elaborate mechanism for how E. coli Mfd, a transcription repair coupling factor, disassembles the RNA polymerase transcription elongation complex to initiate transcription-coupled repair.