In Vitro Insertion and Assembly of Outer Membrane Protein PhoE of Escherichia coli K-12 into the Outer Membrane
نویسندگان
چکیده
منابع مشابه
Assembly of TolC, a structurally unique and multifunctional outer membrane protein of Escherichia coli K-12.
TolC is a multifunctional outer membrane protein of Escherichia coli that folds into a novel alpha-beta-barrel conformation absent in the other model outer membrane proteins used in assembly studies. The data presented in this work show that the unique folded structure of TolC reflects a unique assembly pathway. During its assembly, the newly translocated nascent TolC monomers are released in t...
متن کاملIncreased efficiency of the outer membrane PhoE protein pore in Escherichia coli K-12 mutants with heptose-deficient lipopolysaccharide.
The pore properties of PhoE protein channels in the outer membrane of a lipoprotein-deficient mutant and in a mutant with heptose-deficient lipopolysaccharide were investigated. The absence of lipoprotein neither affects the rate of permeation of glucose 6-phosphate or of the beta-lactam antibiotic cephsulodin through the PhoE pore nor the inhibition of cephsulodin permeation by polyphosphate. ...
متن کاملExport and localization of N-terminally truncated derivatives of Escherichia coli K-12 outer membrane protein PhoE.
To identify export and sorting information in outer membrane protein PhoE of Escherichia coli K-12, a set of deletions was created, resulting in the removal of N-terminal amino acids of the mature protein. Pulse-chase experiments revealed that some mutant proteins were slowly or not at all processed, but there was not correlation between processing rate and the extent of the deletions. The unpr...
متن کاملPore functioning of outer membrane protein PhoE of Escherichia coli: mutagenesis of the constriction loop L3.
Each monomer of the trimeric outer membrane porin PhoE of Escherichia coli consists of a 16-stranded beta-barrel with short turns at the periplasmic side and large loops at the cell surface. One of these loops, L3, is folded inside the beta-barrel and forms a constriction within the channel. Therefore, it is assumed to play an important role in the permeability properties of this general diffus...
متن کاملPrimary structure of major outer membrane protein II (ompA protein) of Escherichia coli K-12.
The amino acid sequence of major outer membrane protein II (ompA protein) from Escherichia coli K-12 has been determined. The transmembrane polypeptide consists of 325 residues, resulting in a molecular weight of 35,159. The transmembrane part of the protein is located between residues 1 and 177. In this part of the protein a predominantly lipophilic 27-residue segment exists that perhaps spans...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1996
ISSN: 0021-9258
DOI: 10.1074/jbc.271.22.12885