Disease relevance of ECs1739

• Evasion of protective immunity by Borrelia burgdorferi by truncation of outer surface protein B [1].
• Thus, the DinR protein is structurally and functionally analogous to the E. coli LexA protein, and accordingly, we propose renaming the protein B. subtilis LexA [2].
• Structure-function relationships in the transposition protein B of bacteriophage Mu [3].
• Antibodies raised against the cloned CAMP cohemolysin cross-reacted with Streptococcus agalactiae protein B. We designate the 27,000-dalton molecule CAMP factor protein and name its corresponding gene cfp [4].
• Use of an isogenic mutant constructed in Moraxella catarrhalis To identify a protective epitope of outer membrane protein B1 defined by monoclonal antibody 11C6 [5].

High impact information on ECs1739

• Histone-like protein H1 (H-NS), DNA supercoiling, and gene expression in bacteria [6].
• Protein H1 is one of the most abundant components of bacterial chromatin and binds to DNA in a relatively nonspecific fashion [6].
• Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B [7].
• Protein B1 contains two types of allosteric binding sites [8].
• The alpha2 dimer (= protein B1) was purified from Escherichia coli B infected with T4 mutant nrdB55 (Yeh, Y.C., and Tessman, I. (1972) Virology 47, 767-772) which carries an amber mutation in the gene coding for the beta polypeptide chain [9].

Chemical compound and disease context of ECs1739

• Overexpression of the divalent cation-regulated outer membrane protein H1 of Pseudomonas aeruginosa is associated with resistance to polymyxin B, aminoglycosides, and EDTA [10].
• Inactivation of the regulatory protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath) by proteolysis can be overcome by a Gly to Gln modification [11].
• In vitro processing of the proproteins GrdE of protein B of glycine reductase and PrdA of D-proline reductase from Clostridium sticklandii: formation of a pyruvoyl group from a cysteine residue [12].
• Methylococcus capsulatus (Bath) uses a soluble methane monooxygenase (sMMO) to catalyse the oxidation of methane to methanol. sMMO is comprised of three components; A, B and C. Protein C (the reductase) transfers electrons from NADH to protein A (the hydroxylase) which contains the active site, and protein B regulates this electron flow [13].

Biological context of ECs1739

• Protein B1 contained binding sites for dATP, an allosteric effector of the reductase [9].
• Protein H1: a role for chromatin structure in the regulation of bacterial gene expression and virulence [14]?
• One of the known targets of histone-like protein H1 is flhDC, the master operon which is absolutely required for flagellar expression [15].
• The reasons for the high stereospecificity of the reaction and the possible structure of the allosteric site of protein B1 are discussed [16].
• This suggests a direct interaction between the two paralogues and the existence of distinct regulons of H-NS and an H-NS/StpA heteromeric complex. hns mutation resulted in increased expression of alpha-hemolysin, fimbriae, and iron uptake systems as well as genes involved in stress adaptation [17].

Anatomical context of ECs1739

• The nucleotide sequence of the rfb gene encoding protein B has been determined, confirming it to be a 697-amino acid protein of 78.9 kDa predicted to be located in the cytoplasmic membrane [18].
• At a high infection dose, hns mutants trigger more sudden lethality due to their increased acute toxicity in murine urinary tract infection and sepsis models [17].
• 3. Cross-linking of cell wall preparations, consisting of the outer membrane and peptidoglycan, showed that protein B and the free form of the lipoprotein, protein F, could be linked to the peptidoglycan [19].

Associations of ECs1739 with chemical compounds

• As an attempt to overcome this problem, I present a kinetic analysis of the folding of a membrane protein, disulfide bond reducing protein B (DsbB), in a mixed micelle system consisting of varying molar ratios of sodium dodecyl sulfate (SDS) and dodecyl maltoside (DM) [20].
• Binding of protein B1 to dTTP or dATP covalently coupled to Sepharose and elution with concentration gradients of the different nucleoside triphosphate effectors gave information about (1) the arrangement of the effector binding sites on protein B1 and (2) the affinity of the effectors for these sites [21].
• Lipopolysaccharide-free protein H1 was purified in high yield by preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis and was subjected to N-terminal amino sequencing [10].

Analytical, diagnostic and therapeutic context of ECs1739

• Surfactant protein mRNA and protein pool sizes were affected differently according to the timing of endotoxin treatment, but a large increase in the amount of mature surfactant protein B in alveolar lavage samples was observed in all endotoxin groups [22].
• Affinity chromatography on anti-B1 monoclonal gels for purification and characterization of protein B1 from Escherichia coli ribonucleotide reductase [23].
• Cross-linking of dTTP to protein B1 by direct photoaffinity labeling, as well as the isolation and sequence determination of the labeled tryptic peptide, has recently been reported [Eriksson, S., Sjöberg, B.-M., Jörnwall, H., & Carlquist, M. (1986) J. Biol. Chem. 261, 1878-1882] [16].
• The introduction of frameshift mutations within the region encoding protein B resulted in the synthesis of an antigenically altered LPS which is shorter than the wild-type LPS, as assessed by reaction to antisera in colony and Western immunoblots, and by silver staining of LPS separated on sodium dodecyl sulfate-polyacrylamide-gel electrophoresis [18].
• Infected bacteria synthesize the replication protein B (MR 33000) of Mu, which was found by cell fractionation experiments to be associated with the inner cell membrane [24].

References