Isolation and characterization of deletion mutants of ompR and envZ, regulatory genes for expression of the outer membrane proteins OmpC and OmpF in Escherichia coli.

Isolation and characterization of deletion mutants of ompR and envZ, regulatory genes for expression of the outer membrane proteins OmpC and OmpF in Escherichia coli. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Isolation and characterization of deletion mutants of ompR and envZ, regulatory genes for expression of the outer membrane proteins OmpC and OmpF in Escherichia coli. Abstract Text:

T Mizuno,S Mizushima,

Expression of the ompC and ompF genes coding for the major outer membrane proteins, OmpC and OmpF, respectively, is known to be controlled by at least two regulatory genes, ompR and envZ, which together comprise a single ompB operon. We constructed chromosomal mutants with either ompR-envZ deletion or envZ deletion. Characterization of these deletion strains showed that the OmpR protein is necessary for transcription of the ompC and ompF genes, and the EnvZ protein is essential for normal regulation of the ompC and ompF expression, which is affected by the medium osmolarity. We also constructed several plasmids carrying different portions of the ompB operon. Characterization of these plasmids allowed us to identify the OmpR protein with an apparent molecular weight of 29 kilodaltons (kDa) and the EnvZ protein with an apparent molecular weight of 50 kDa. The initiation codon for EnvZ translation appeared to overlap with the termination codon for OmpR translation. It was also found that a truncated EnvZ polypeptide (44 kDa) which lacks the N-terminal 55 amino acid residues can complement the envZ deletion mutant. Based on these results, the structure and function of the ompB operon are discussed in relation to the regulation of ompC and ompF expression.

Isolation and characterization of deletion mutants of ompR and envZ, regulatory genes for expression of the outer membrane proteins OmpC and OmpF in Escherichia coli. Publishing Authors By Initials

T Mizuno,S Mizushima,

For similar genetic structures: plasmids research abstracts see: genetic structures: plasmids research

PUBMED ID PMID:

MEDLINE DATE:

Isolation and characterization of deletion mutants of ompR and envZ, regulatory genes for expression of the outer membrane proteins OmpC and OmpF in Escherichia coli. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 101

Page Numbers: 387-96

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Feb

YEAR: 1987

Isolation and characterization of deletion mutants of ompR and envZ, regulatory genes for expression of the outer membrane proteins OmpC and OmpF in Escherichia coli. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Isolation and characterization of deletion mutants of ompR and envZ, regulatory genes for expression of the outer membrane proteins OmpC and OmpF in Escherichia coli. Keywords Mesh Terms:

KEYWORDS: Plasmids

MESH TERMS: isolation & purification

Chemical & Substance for Abstract: Isolation and characterization of deletion mutants of ompR and envZ, regulatory genes for expression of the outer membrane proteins OmpC and OmpF in Escherichia coli. Information

Substance Name: Bacterial Outer Membrane Proteins

Registry Number: 0

Grant and Affiliation Information for Isolation and characterization of deletion mutants of ompR and envZ, regulatory genes for expression of the outer membrane proteins OmpC and OmpF in Escherichia coli.

AFFILIATION:

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Isolation and characterization of deletion mutants of ompR and envZ, regulatory genes for expression of the outer membrane proteins OmpC and OmpF in Escherichia coli Related Publications

• Acidic phospholipids with unsaturated fatty acids inhibit the binding of origin recognition complex to origin DNA.
• Arrangement of bacteriophage lambda receptor protein (LamB) in the Escherichia coli cell surface.
• Arrangement of bacteriophage lambda receptor protein (LamB) in the cell surface of Escherichia coli: a reconstitution study.
• Autophagy: process and function.
• Characterization of major outer membrane proteins O-8 and O-9 of Escherichia coli K-12. Evidence that structural genes for the two proteins are different.
• Effects of heating in dodecyl sulfate solution on the conformation and electrophoretic mobility of isolated major outer membrane proteins from Escherichia coli K-12.
• Identification of an outer membrane protein responsible for the binding of the Fe-enterochelin complex to Escherichia coli cells.
• Inhibition of vesicle-mediated protein transport by nordihydroguaiaretic acid.
• Insertion of a signal peptide-derived hydrophobic segment into the mature domain of OmpC, an outer membrane protein, does not interfere with the export of the following polypeptide chain across the cytoplasmic membrane of E. coli.
• Interaction between ORC and Cdt1p of Saccharomyces cerevisiae.
• Interactions of outer membrane proteins O-8 and O-9 with peptidoglycan sacculus of Escherichia coli K-12.
• Involvement of outer membrane proteins in enterochelin-mediated iron uptake in Escherichia coli.
• Involvement of prostaglandin E2 in production of amyloid-beta peptides both in vitro and in vivo.
• Isolation and characterization of deletion mutants of ompR and envZ, regulatory genes for expression of the outer membrane proteins OmpC and OmpF in Escherichia coli.
• Lipoprotein-bearing peptidoglycan sacculus as a preferred site for the in vitro assembly of membrane from dissociated components of outer membrane of Escherichia coli K-12.
• Membrane ATPase of Bacillus megaterium. I. Properties of membrane ATPase and its solubilized form.
• Molecular assembly of the lipoprotein trimer on the peptidoglycan layer of Escherichia coli.
• Purification and characterization of a signal peptide, a product of protein secretion across the cytoplasmic membrane of Escherichia coli.
• Purification and properties of membrane bound NADH2 dehydrogenase in Bacillus megaterium.
• Removal by bovine serum albumin of fatty acids from membrane vesicles and its effect on proline transport activity in Escherichia coli.
• Sequence-independent DNA binding activity of DnaA protein, the initiator of chromosomal DNA replication in Escherichia coli.
• Site-directed mutational analysis of DnaA protein, the initiator of chromosomal DNA replication in E. coli.
• Spectral characteristics of yeast cytochrome c's at the temperature of liquid nitrogen.
• Strain specificity of outer membrane proteins in Escherichia coli.
• The hydrophobic region of signal peptides is a determinant for SRP recognition and protein translocation across the ER membrane.
• The membrane ATPase of Bacillus megaterium. II. Purification of membrane ATPases and their recombination with membrane.
• Use of a series of ompF-ompC chimeric proteins for locating antigenic determinants recognized by monoclonal antibodies against the ompC and ompF proteins of the Escherichia coli outer membrane.
• Yeast two-hybrid analysis of the origin recognition complex of Saccharomyces cerevisiae: interaction between subunits and identification of binding proteins.
• [Induction of HO-1 by NSAIDs and its role in NSAID-induced gastric ulcers]
• [Protection of gastrointestinal mucosa against NSAID-induced ulcer]