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.

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. Research Abstract Details 

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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. Abstract Text:

M N Hall,M Schwartz,T J Silhavy,

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. Publishing Authors By Initials

MN Hall,M Schwartz,TJ Silhavy,

For similar enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: galactosidases: beta-galactosidase research abstracts see: enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: galactosidases: beta-galactosidase research

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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. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Journal of molecular biology

VOLUME: 156

Page Numbers: 93-112

Journal Abbreviation: J. Mol. Biol.

ISSN: 0022-2836

DAY: 25

MONTH: Mar

YEAR: 1982

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. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985088

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. Keywords Mesh Terms:

KEYWORDS: beta-Galactosidase

MESH TERMS: biosynthesis

Chemical & Substance for Abstract: 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. Information

Substance Name: beta-Galactosidase

Registry Number: EC 3.2.1.23

Grant and Affiliation Information for 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.

AFFILIATION:

Country: ENGLAND

AGENCY: United States NCI

GRANT: N01-CO-75380

ACRONYM: CO

MEDLINETA: J Mol Biol

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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 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.