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  • Influence
Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter.
We have constructed a series of plasmid vectors (pBAD vectors) containing the PBAD promoter of the araBAD (arabinose) operon and the gene encoding the positive and negative regulator of thisExpand
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Identification of a protein required for disulfide bond formation in vivo
We describe a mutation (dsbA) that renders Escherichia coli severely defective in disulfide bond formation. In dsbA mutant cells, pulse-labeled beta-lactamase, alkaline phosphatase, and OmpA areExpand
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TnphoA: a transposon probe for protein export signals.
  • C. Manoil, J. Beckwith
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences…
  • 1 December 1985
We constructed a derivative of transposon Tn5 that permits the generation of hybrid proteins composed of alkaline phosphatase (EC 3.1.3.1) lacking its signal peptide fused to amino-terminal sequencesExpand
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Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status.
The Escherichia coli transcription factor OxyR is activated by the formation of an intramolecular disulfide bond and subsequently is deactivated by enzymatic reduction of the disulfide bond. Here weExpand
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Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system.
We show that the two-component signal transduction system of Escherichia coli, CpxA-CpxR, controls the expression of genes encoding cell envelope proteins involved in protein folding and degradation.Expand
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Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL.
Assembly of the division septum in bacteria is mediated by several proteins that localize to the division site. One of these, FtsI (also called penicillin-binding protein 3) of Escherichia coli,Expand
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Diverse Paths to Midcell: Assembly of the Bacterial Cell Division Machinery
At the heart of bacterial cell division is a dynamic ring-like structure of polymers of the tubulin homologue FtsZ. This ring forms a scaffold for assembly of at least ten additional proteins atExpand
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A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region
Summary Three membrane proteins required for cell division in Escherichia coli, FtsQ, FtsL and FtsB, localize to the cell septum. FtsL and FtsB, which each contain a leucine zipper‐like sequence, areExpand
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FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co‐localization with FtsZ during Escherichia coli cell division
During cell division in Gram‐negative bacteria, the cell envelope invaginates and constricts at the septum, eventually severing the cell into two compartments, and separating the replicated geneticExpand
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Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature.
The degP gene, required for proteolysis in the cell envelope of Escherichia coli, maps at approximately 3.5 min on the chromosome. Null mutations in degP result in temperature-sensitive growth. InExpand
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