A genetic approach for analyzing the pathway of LamB assembly into the outer membrane of Escherichia coli.

A genetic approach for analyzing the pathway of LamB assembly into the outer membrane of Escherichia coli. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

A genetic approach for analyzing the pathway of LamB assembly into the outer membrane of Escherichia coli. Abstract Text:

R Misra,A Peterson,T Ferenci,T J Silhavy,

Results presented in this study demonstrate that a mutation which inserts an additional tyrosine between the 2 tyrosines at residues 118 and 119 of mature LamB protein results in a temperature-dependent assembly defect. This defect leads to the accumulation of an intermediate at the restrictive temperature that is most likely an assembly-defective monomer. These monomers are rapidly degraded in the wild type (htrA+) strain, and the biphasic kinetics of this degradation indicate that the mutation affects the assembly process and not the final product, i.e. stable trimers. In addition, our data show that the temperature-dependent assembly defect in the mutant strain is reversible, and therefore the accumulated monomers represent a true assembly intermediate. Fractionation studies show that the monomers, which can be accumulated in htrA (degP) mutants at the restrictive temperature, are associated with the outer membrane, indicating that trimerization of LamB is not a prerequisite for localization.

A genetic approach for analyzing the pathway of LamB assembly into the outer membrane of Escherichia coli. Publishing Authors By Initials

R Misra,A Peterson,T Ferenci,TJ Silhavy,

For similar environment and public health: environment: environment, controlled: temperature research abstracts see: environment and public health: environment: environment, controlled: temperature research

PUBMED ID PMID:

MEDLINE DATE:

A genetic approach for analyzing the pathway of LamB assembly into the outer membrane of Escherichia coli. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: The Journal of biological chemistry

VOLUME: 266

Page Numbers: 13592-7

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 25

MONTH: Jul

YEAR: 1991

A genetic approach for analyzing the pathway of LamB assembly into the outer membrane of Escherichia coli. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

A genetic approach for analyzing the pathway of LamB assembly into the outer membrane of Escherichia coli. Keywords Mesh Terms:

KEYWORDS: Temperature

MESH TERMS: metabolism

Chemical & Substance for Abstract: A genetic approach for analyzing the pathway of LamB assembly into the outer membrane of Escherichia coli. Information

Substance Name: maltose-binding protein

Registry Number: 0

Grant and Affiliation Information for A genetic approach for analyzing the pathway of LamB assembly into the outer membrane of Escherichia coli.

AFFILIATION: Department of Molecular Biology, Lewis Thomas Laboratory, Princeton University, New Jersey 08544-1014.

Country: UNITED STATES

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biol Chem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

A genetic approach for analyzing the pathway of LamB assembly into the outer membrane of Escherichia coli Related Publications

• A genetic approach for analyzing the pathway of LamB assembly into the outer membrane of Escherichia coli.
• A progenitor of the outer membrane LamB trimer.
• CpxP, a stress-combative member of the Cpx regulon.
• Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli.
• Enhanced export of beta-galactosidase fusion proteins in prlF mutants is Lon dependent.
• Folding-based suppression of extracytoplasmic toxicity conferred by processing-defective LamB.
• Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli.
• Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli.
• Importance of secondary structure in the signal sequence for protein secretion.
• Information within the mature LamB protein necessary for localization to the outer membrane of E coli K12.
• Inter-kingdom conservation of mechanism of nonsense-mediated mRNA decay.
• Intragenic regions required for LamB export.
• Kinetic analysis of lamB mutants suggests the signal sequence plays multiple roles in protein export.
• Kinetic analysis of the assembly of the outer membrane protein LamB in Escherichia coli mutants each lacking a secretion or targeting factor in a different cellular compartment.
• Molecular components of the signal sequence that function in the initiation of protein export.
• Null mutations in a Nudix gene, ygdP, implicate an alarmone response in a novel suppression of hybrid jamming.
• PrlA and PrlG suppressors reduce the requirement for signal sequence recognition.
• Probing the barrier function of the outer membrane with chemical conditionality.
• Quality control in the bacterial periplasm.
• Secretion of LamB-LacZ by the signal recognition particle pathway of Escherichia coli.
• Sequence information within the lamB genes in required for proper routing of the bacteriophage lambda receptor protein to the outer membrane of Escherichia coli K-12.
• Signal sequence mutations as tools for the characterization of LamB folding intermediates.
• Signal sequence processing is required for the assembly of LamB trimers in the outer membrane of Escherichia coli.
• Suppressor mutations that restore export of a protein with a defective signal sequence.
• Tethering of CpxP to the inner membrane prevents spheroplast induction of the cpx envelope stress response.
• The first 28 amino acids of mature LamB are required for rapid and efficient export from the cytoplasm.
• The sigma(E) and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli.
• The sigmaE and Cpx regulatory pathways: overlapping but distinct envelope stress responses.
• Two cellular components, PrlA and SecB, that recognize different sequence determinants are required for efficient protein export.