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Article

A fraction of the BglG transcriptional antiterminator from Escherichia coli exists as a compact monomer.

The Journal of biological chemistry - 19 Dec 2003

Fux Liat, Nussbaum-Shochat Anat, Amster-Choder Orna

Abstract excerpt

Expression of the bgl operon in Escherichia coli, induced by beta-glucosides, is positively regulated by BglG, a transcriptional antiterminator. In the presence of inducer, BglG dimerizes and binds to the bgl transcript to prevent premature termination of transcription. The dimeric state of BglG is determined by BglF, a membrane-bound enzyme II of the phosphoenolpyruvate-dependent phosphotransferase system (PTS),...

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Source

Identifiers

PMID: 14514681
DOI: 10.1074/jbc.M308085200

Genes

PTS

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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A fraction of the BglG transcriptional antiterminator from Escherichia coli exists as a compact monomer.PMID 14514681Read ↗

Dimer stabilization upon activation of the transcriptional antiterminator LicT.Semantic proximity Read ↗

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Regulation of the Escherichia coli antiterminator protein BglG by phosphorylation at multiple sites and evidence for transfer of phosphoryl groups between monomers.Semantic proximity Read ↗

Crystal structure of an activated form of the PTS regulation domain from the LicT transcriptional antiterminator.Semantic proximity Read ↗

Experimental and computational characterization of the dimerization of the PTS-regulation domains of BglG from Escherichia coli.Semantic proximity Read ↗

Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes.Semantic proximity Read ↗

Folding and association of beta-Galactosidase.Semantic proximity Read ↗

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