Isolation and analysis of novel mutants of Escherichia coli prlA (secY).
Plasmid libraries of prlA mutants containing single-base-pair changes throughout the gene were generated by in vitro random mutagenesis. The prlA mutations capable of suppressing the secretion defect of LamB caused by mutations in the LamB signal peptide were selected and analyzed. Together with additional mutations generated by site-directed mutagenesis, a number of novel prlA mutations and/or suppressors were identified. These mutations provide the starting points for studying the relationship of structure and function of PrlA in its interaction with LamB and/or other component(s) in the Escherichia coli protein secretion-translocation complex.
Olsen
M K
MK
Upjohn Company, Kalamazoo, Michigan 49007.
Rosey
E L
EL
Tomich
C S
CS
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics* / Q000302:isolation & purification; D029968:Escherichia coli Proteins; D015723:Gene Library; D005798:Genes, Bacterial; D016297:Mutagenesis, Site-Directed; D010957:Plasmids; D018272:Porins; D021382:Protein Sorting Signals / Q000096:biosynthesis / Q000235:genetics; D017433:Protein Structure, Secondary; D011991:Receptors, Virus / Q000096:biosynthesis; D015183:Restriction Mapping; D000069816:SEC Translocation Channels; D013489:Suppression, Genetic
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D018272:Porins; D021382:Protein Sorting Signals; D011991:Receptors, Virus; D000069816:SEC Translocation Channels; C057841:SecY protein, E coli; C016532:maltoporins