Molecular components of the signal sequence that function in the initiation of protein export.

Molecular components of the signal sequence that function in the initiation of protein export. Research Abstract Details 

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Molecular components of the signal sequence that function in the initiation of protein export. Abstract Text:

S D Emr,T J Silhavy,

We are studying the mechanism by which the LamB protein is exported to the outer membrane of Escherichia coli. Using two selection procedures based on gene fusions, we have identified a number of mutations that cause alterations in the LamB signal sequence. Characterization of the mutant strains revealed that although many such mutations block LamB export to greater than 95%, others have essentially no effect. These results allow an analysis of the functions performed by the various molecular components of the signal sequence. Our results suggest that a critical subset of four amino acids is contained within the central hydrophobic core of the LamB signal sequence. If this core can assume an alpha-helical conformation, these four amino acids comprise a recognition site that interacts with a component of the cellular export machinery. Since mechanisms of protein localization appear to have been conserved during evolution, the principles established by these results should be applicable to similar studies in eukaryotic cells.

Molecular components of the signal sequence that function in the initiation of protein export. Publishing Authors By Initials

SD Emr,TJ Silhavy,

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

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Molecular components of the signal sequence that function in the initiation of protein export. Journal Published:

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

Journal: The Journal of cell biology

VOLUME: 95

Page Numbers: 689-96

Journal Abbreviation: J. Cell Biol.

ISSN: 0021-9525

DAY: 27

MONTH: Dec

YEAR: 1982

Molecular components of the signal sequence that function in the initiation of protein export. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 375356

Molecular components of the signal sequence that function in the initiation of protein export. Keywords Mesh Terms:

KEYWORDS: Receptors, Virus

MESH TERMS: metabolism

Chemical & Substance for Abstract: Molecular components of the signal sequence that function in the initiation of protein export. Information

Substance Name: maltoporins

Registry Number: 0

Grant and Affiliation Information for Molecular components of the signal sequence that function in the initiation of protein export.

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Country: UNITED STATES

AGENCY: United States NCI

GRANT: N01-CO-75380

ACRONYM: CO

MEDLINETA: J Cell Biol

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Molecular components of the signal sequence that function in the initiation of protein export 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.
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• 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.