Insertion of a MalE beta-galactosidase fusion protein into the envelope of Escherichia coli disrupts biogenesis of outer membrane proteins and processing of inner membrane proteins.

Insertion of a MalE beta-galactosidase fusion protein into the envelope of Escherichia coli disrupts biogenesis of outer membrane proteins and processing of inner membrane proteins. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Insertion of a MalE beta-galactosidase fusion protein into the envelope of Escherichia coli disrupts biogenesis of outer membrane proteins and processing of inner membrane proteins. Abstract Text:

E Herrero,M Jackson,P J Bassford,D Sinden,I B Holland,

The synthesis of a membrane-bound MalE beta-galactosidase hybrid protein, when induced by growth of Escherichia coli on maltose, leads to inhibition of cell division and eventually a reduced rate of mass increase. In addition, the relative rate of synthesis of outer membrane proteins, but not that of inner membrane proteins, was reduced by about 50%. Kinetic experiments demonstrated that this reduction coincided with the period of maximum synthesis of the hybrid protein (and another maltose-inducible protein, LamB). The accumulation of this abnormal protein in the envelope therefore appeared specifically to inhibit the synthesis, the assembly of outer membrane proteins, or both, indicating that the hybrid protein blocks some export site or causes the sequestration of some limiting factor(s) involved in the export process. Since the MalE protein is normally located in the periplasm, the results also suggest that the synthesis of periplasmic and outer membrane proteins may involve some steps in common. The reduced rate of synthesis of outer membrane proteins was also accompanied by the accumulation in the envelope of at least one outer membrane protein and at least two inner membrane proteins as higher-molecular-weight forms, indicating that processing (removal of the N-terminal signal sequence) was also disrupted by the presence of the hybrid protein. These results may indicate that the assembly of these membrane proteins is blocked at a relatively late step rather than at the level of primary recognition of some site by the signal sequence. In addition, the results suggest that some step common to the biogenesis of quite different kinds of envelope protein is blocked by the presence of the hybrid protein.

Insertion of a MalE beta-galactosidase fusion protein into the envelope of Escherichia coli disrupts biogenesis of outer membrane proteins and processing of inner membrane proteins. Publishing Authors By Initials

E Herrero,M Jackson,PJ Bassford,D Sinden,IB Holland,

For similar proteins: membrane proteins: receptors, cell surface: receptors, virus research abstracts see: proteins: membrane proteins: receptors, cell surface: receptors, virus research

PUBMED ID PMID:

MEDLINE DATE:

Insertion of a MalE beta-galactosidase fusion protein into the envelope of Escherichia coli disrupts biogenesis of outer membrane proteins and processing of inner membrane proteins. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of bacteriology

VOLUME: 152

Page Numbers: 133-9

Journal Abbreviation: J. Bacteriol.

ISSN: 0021-9193

DAY: 27

MONTH: Oct

YEAR: 1982

Insertion of a MalE beta-galactosidase fusion protein into the envelope of Escherichia coli disrupts biogenesis of outer membrane proteins and processing of inner membrane proteins. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985120

Insertion of a MalE beta-galactosidase fusion protein into the envelope of Escherichia coli disrupts biogenesis of outer membrane proteins and processing of inner membrane proteins. Keywords Mesh Terms:

KEYWORDS: Receptors, Virus

MESH TERMS: biosynthesis

Chemical & Substance for Abstract: Insertion of a MalE beta-galactosidase fusion protein into the envelope of Escherichia coli disrupts biogenesis of outer membrane proteins and processing of inner membrane proteins. Information

Substance Name: Maltose

Registry Number: 69-79-4

Grant and Affiliation Information for Insertion of a MalE beta-galactosidase fusion protein into the envelope of Escherichia coli disrupts biogenesis of outer membrane proteins and processing of inner membrane proteins.

AFFILIATION:

Country: UNITED STATES

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Bacteriol

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Insertion of a MalE beta-galactosidase fusion protein into the envelope of Escherichia coli disrupts biogenesis of outer membrane proteins and processing of inner membrane proteins Related Publications

• 2-Methoxycanthin-6-one: A New Alkaloid from the Stem Wood of Quassia amara.
• A dinucleating ligand related to the beta-diketiminates.
• Adjunctive treatment of disseminated Mycobacterium avium complex infection with interferon alpha-2b in a patient with complete interferon-gamma receptor R1 deficiency.
• AmphiBMP2/4, an amphioxus bone morphogenetic protein closely related to Drosophila decapentaplegic and vertebrate BMP2 and BMP4: insights into evolution of dorsoventral axis specification.
• Attitudes to the use of prophylaxis for thrombo-embolism in neurosurgical patients.
• Binding affinity of alkynes and alkenes to low-coordinate iron.
• Cap gun burns in children.
• Characterization of anisotropic myocardial backscatter using spectral slope, intercept and midband fit parameters.
• Cis-regulation of the amphioxus engrailed gene: insights into evolution of a muscle-specific enhancer.
• Cytokines and other immunological biomarkers in children's environmental health studies.
• Dissociable effects of disconnecting amygdala central nucleus from the ventral tegmental area or substantia nigra on learned orienting and incentive motivation.
• Expression of Th1/Th2 cytokines in human blood after in vitro treatment with chlorpyrifos, and its metabolites, in combination with endotoxin LPS and allergen Der p1.
• Fulminant mulch pneumonitis: an emergency presentation of chronic granulomatous disease.
• Functional magnetic resonance imaging of hearing-impaired children under sedation before cochlear implantation.
• Global and local development of gray and white matter volume in normal children and adolescents.
• Insertion of a MalE beta-galactosidase fusion protein into the envelope of Escherichia coli disrupts biogenesis of outer membrane proteins and processing of inner membrane proteins.
• Learned contextual cue potentiates eating in rats.
• Magnetic resonance imaging determination of tumor grade and early response to temozolomide in a genetically engineered mouse model of glioma.
• Mechanistic insight into N=N cleavage by a low-coordinate iron(II) hydride complex.
• Mouse models of brain tumors and their applications in preclinical trials.
• Notch signaling enhances nestin expression in gliomas.
• Platelet-derived growth factor-mediated gliomagenesis and brain tumor recruitment.
• Quantitative geometric descriptions of the belt iron atoms of the iron-molybdenum cofactor of nitrogenase and synthetic iron(II) model complexes.
• Rapid viral quasispecies evolution: implications for vaccine and drug strategies.
• Reinforcer-specificity of appetitive and consummatory behavior of rats after Pavlovian conditioning with food reinforcers.
• Sex differences in the development of neuroanatomical functional connectivity underlying intelligence found using Bayesian connectivity analysis.
• Sinking velocities of phytoplankton measured on a stable density gradient by laser scanning.
• Survey of Connecticut Nurse-Midwives.
• Testicular nubbins and prosthesis insertion: is it all just in the timing?
• Winter travel assignments appeal to RN, ski bum.