Mutations altering the cellular localization of the phage lambda receptor, an Escherichia coli outer membrane protein.
AUTOR(ES)
Emr, S D
RESUMO
Two mutant strains of Escherichia coli have been isolated in which the cellular location of an outer membrane protein, the phage lambda receptor (the lamB gene product), is altered. These mutations were initially selected in a strain containing a lamB-lacZ fusion. In the parent strain the protein coded for by the hybrid gene is located, at least in part, in the outer membrane. In the mutants it is located in the cytoplasm. 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. One of these mutations is a small deletion internal to the lamB gene. When this mutation is present in an otherwise wild-type lamB gene, the protein produced is of lower molecular weight than normal receptor. The other mutation behaves as a point mutation; when it is present in an otherwise normal lamB gene, reversion can be demonstrated. The molecular weight of this mutant protein, which is located in the cytoplasm, is larger than that of the wild-type gene product by approximately 2000. It is suggested that these two mutations are in the portion of the lamB gene coding for a signal sequence and thereby block export of the protein.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=393063Documentos Relacionados
- DNA sequence encoding the NH2-terminal peptide involved in transport of lambda receptor, an Escherichia coli secretory protein.
- Cellular localization of the Escherichia coli SpoT protein.
- Signal sequence mutations that alter coupling of secretion and translation of an Escherichia coli outer membrane protein.
- Cloning and Expression of the Escherichia coli K1 Outer Membrane Protein A Receptor, a gp96 Homologue
- Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein.