Membrane Localization of the HflA Regulatory Protease of Escherichia Coli by Immunoelectron Microscopy

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1991 Oct 1

PMID 1833381

Citations 6

Authors

T S Zorick

H Echols

Affiliations

Soon will be listed here.

Abstract

The hflA locus of Escherichia coli specifies a multisubunit protease that selectively degrades the cII transcriptional activator of phage lambda. The regulated turnover of cII is critical for the choice between the lytic and lysogenic pathways of viral development. Previous cell fractionation work has indicated that HflA is associated with the inner membrane fraction. We have sought to demonstrate that the HflA protease is localized in the cell membrane of intact cells. To achieve this goal, we have combined electron microscopy of thin-sectioned E. coli cells with antibody tagging by a colloidal gold label. Using antibody to purified HflA protein, we have found preferential membrane labeling for hflA+ cells but not for hflA mutant cells. We conclude that HflA protease is localized in the cell membrane. The membrane location for HflA protein may serve as a component of a targeting mechanism to limit the action of the regulatory protease to selected cytoplasmic proteins.

Citing Articles

Studies on Escherichia coli HflKC suggest the presence of an unidentified λ factor that influences the lysis-lysogeny switch.

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Stochastic kinetic analysis of developmental pathway bifurcation in phage lambda-infected Escherichia coli cells.

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Host regulation of lysogenic decision in bacteriophage lambda: transmembrane modulation of FtsH (HflB), the cII degrading protease, by HflKC (HflA).

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A protease complex in the Escherichia coli plasma membrane: HflKC (HflA) forms a complex with FtsH (HflB), regulating its proteolytic activity against SecY.

Kihara A, Akiyama Y, Ito K EMBO J. 1996; 15(22):6122-31.

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The Escherichia coli hflA locus encodes a putative GTP-binding protein and two membrane proteins, one of which contains a protease-like domain.

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