Disease relevance of lamB

• Using larger liposomes prepared by the fusion of lamB bearing vesicles with polyethylene glycol and n-hexyl bromide, the heads of most of the bound bacteriophage appeared to be completely empty of DNA [1].
• These were cloned in frame into the lamB gene of the Escherichia coli expression vector pAJC264 [2].

High impact information on lamB

• We show that, under certain conditions, in a strain diploid for gene lamB, all the missense lamB mutations conferring lambda resistance that we have tested are dominant with respect to wild-type [3].
• Negative dominance in gene lamB: random assembly of secreted subunits issued from different polysomes [3].
• Genetic study of a membrane protein: DNA sequence alterations due to 17 lamB point mutations affecting adsorption of phage lambda [4].
• In a liposome swelling assay designed to measure rates of diffusion, the lamB protein conferred permeability to phospholipid liposomes for a variety of substrates [5].
• The mutations responsible for the alteration of cellular location lie very early in the lamB gene, in a region corresponding to the NH2-terminus of the lambda receptor protein [6].

Chemical compound and disease context of lamB

• Chemotaxis towards maltose is specifically defective in many strains of Escherichia coli carrying mutations affecting lamB, the gene coding for the outer membrane receptor for bacteriophage lambda [7].

Biological context of lamB

• Rather, the improvement in glucose scavenging involves induction of genes in 2 distinct regulons (mgl/gal and mal/lamB) through synthesis of 2 different endogenous inducer molecules (galactose, maltotriose) [8].
• An analysis of the first set of 16 clones constructed by this technique shows that, in these clones, the lamB protein is altered either by frameshift mutations leading to abnormal COOH terminal (usually premature termination) or by in-phase deletions or small insertions [9].
• Linker mutagenesis in the gene of an outer membrane protein of Escherichia coli, lamB [9].
• These mutations can be placed into three classes based on the degree to which they suppress the lamB signal sequence deletion, lamBs78 [10].
• In the resulting strains, the expression of two of the maltose operons, malEFG and malK-lamB, still required the action of CAP, whereas that of the third operon, malPQ, was CAP independent [11].

Associations of lamB with chemical compounds

• In agreement with the fact that the lambda h mutants (and the lambda hh* mutants) could grow on all of the lamB class I mutations tested, we found tha the nature of the J mutations did not depend on the LamB class I mutant used to select them [12].

Analytical, diagnostic and therapeutic context of lamB

• Isolation, by affinity chromatography, of mutant escherichia coli cells with novel regulation of lamB expression [13].
• The procedure consisted of performing immunoprecipitation experiments with extracts of strains which produced truncated fragments of LamB, either in a free form (deletion and nonsense mutants) or fused to another polypeptide (malK-lamB and lamB-lacZ fusion strains) [14].

References