Negative dominance in gene lamB: random assembly of secreted subunits issued from different polysomes

lamB is the structural gene for the lambda receptor, an oligomeric outer membrane protein from Escherichia coli K12 involved in phage lambda adsorption. We show that, under certain conditions, in a strain diploid for gene lamB, all the missense lamB mutations conferring lambda resistance that we hav...

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Bibliographic Details
Published in:The EMBO journal 1983-01, Vol.2 (1), p.81-86
Main Authors: Marchal, C., Hofnung, M.
Format: Article
Language:English
Subjects:
Bacterial Outer Membrane Proteins - genetics
Escherichia coli
Escherichia coli - genetics
genes
Genes, Bacterial
membrane proteins
missense mutant
phage lambda
Polyribosomes
Porins
receptors
Receptors, Virus - genetics
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Summary:lamB is the structural gene for the lambda receptor, an oligomeric outer membrane protein from Escherichia coli K12 involved in phage lambda adsorption. 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. We propose a model which allows a quantitative interpretation of the data. It is based on negative complementation at the level of oligomerisation. Wild‐type and mutant subunits would assemble at random forming homo‐ and hetero‐oligomers. Only wild‐type homo‐oligomers would be efficient for phage inactivation. For some classes of missense mutations the hetero‐oligomers would have the capacity to bind, but not to inactivate the phage. The model confirms that active lambda receptor is a trimer and implies that for this secreted protein there is no preferential assembly of subunits originating from the same polysome.
ISSN:0261-4189
1460-2075
DOI:10.1002/j.1460-2075.1983.tb01385.x