Role of a disulfide bond in the thermal stability of the LamB protein trimer in Escherichia coli outer membrane.

Role of a disulfide bond in the thermal stability of the LamB protein trimer in Escherichia coli outer membrane. Research Abstract Details 

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Role of a disulfide bond in the thermal stability of the LamB protein trimer in Escherichia coli outer membrane. Abstract Text:

M Luckey,R Ling,A Dose,B Malloy,

In order to understand the unusual heat resistance of LamB protein (the outer membrane component of the maltose transport system in Escherichia coli and its receptor for bacteriophage lambda), we investigated the role of its 2 cysteinyl residues. Our studies show that Cys22 and Cys38 form an intrasubunit disulfide bond which contributes to the heat stability of the LamB protein trimer. Physical evidence for the disulfide was obtained by using site-directed mutagenesis to convert Asn36 to Met, which allowed cyanogen bromide cleavage between the 2 cysteines. Upon reduction one of the N36M fragments migrated as two pieces, resolved by two-dimensional polyacrylamide gel electrophoresis. Other mutagenized LamB proteins, in which 1 or both Cys residues were converted to Ser, exhibited a sharp loss of thermal stability. In contrast to wild-type LamB protein trimer, which does not dissociate to monomers even after 60 min at 100 degrees C, only 10-15% of the mutant LamB proteins remain trimeric after boiling 10 min. The disulfide bond in LamB protein is not required for its transport function, since both mutagenized LamB protein and N-ethylmaleimide-labeled LamB protein exhibit normal uptake of sugars in proteoliposomes. Finally, the disulfide bond must not be between subunits of the LamB trimer since reversible dissociation of trimer is achieved by low pH or denaturants in the absence of reducing agent.

Role of a disulfide bond in the thermal stability of the LamB protein trimer in Escherichia coli outer membrane. Publishing Authors By Initials

M Luckey,R Ling,A Dose,B Malloy,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research

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Role of a disulfide bond in the thermal stability of the LamB protein trimer in Escherichia coli outer membrane. Journal Published:

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

Journal: The Journal of biological chemistry

VOLUME: 266

Page Numbers: 1866-71

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 25

MONTH: Jan

YEAR: 1991

Role of a disulfide bond in the thermal stability of the LamB protein trimer in Escherichia coli outer membrane. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Role of a disulfide bond in the thermal stability of the LamB protein trimer in Escherichia coli outer membrane. Keywords Mesh Terms:

KEYWORDS: Structure-Activity Relationship

MESH TERMS: chemistry

Chemical & Substance for Abstract: Role of a disulfide bond in the thermal stability of the LamB protein trimer in Escherichia coli outer membrane. Information

Substance Name: Sodium Dodecyl Sulfate

Registry Number: 151-21-3

Grant and Affiliation Information for Role of a disulfide bond in the thermal stability of the LamB protein trimer in Escherichia coli outer membrane.

AFFILIATION: Department of Chemistry and Biochemistry, San Francisco State University, California 94132.

Country: UNITED STATES

AGENCY: United States NIAID

GRANT: AI20727

ACRONYM: AI

MEDLINETA: J Biol Chem

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