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• W2149351661 abstract "To Identify elements participating In the process of transformation, a bank of genetically altered mutants of Streptococcus pneumoniae with defects in exported proteins was assessed for a decrease in transformation efficiency. One mutant consistentiy transformed 10-foid less than the parent strain. Sequence analysis and reconstitution of the altered locus revealed a gene, plpA (permease-like protein), which encodes a putative substrate-binding protein belonging to the family of bacterial permeases responsible for peptide transport. The derived amino acid sequence for this gene was 80% similar to AmiA, a peptide-binding protein homologue from pneumococcus, and 50% similar over 230 amino acids to SpooKA which is a regulatory element in the process of transformation and sporulation in Bacillus subtilis. PIpA fusions to alkaline phosphatase (PhoA) were shown to be membrane associated and labelled with [3H]-palmitic acid, which probably serves as a membrane anchor. Experiments designed to define the roles of the pIpA and ami determinants in the process of transformation showed that: (i) mutants with defects in plpA were >90% transformation deficient while ami mutants exhibited up to a fourfold increase in transformation efficiency; (ii) compared to the parental strain, the onset of competence in an ami mutant occurred earlier in logarithmic growth, whereas the onset was delayed in a plpA mutant; and (ill) the plpA mutation decreases the expression of a competence-regulated locus. Since the permease mutants would fail to bind specific ligands, it seems likely that the substrate-permease interaction modulates the process of transformation." @default.
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• W2149351661 date "1994-06-01" @default.
• W2149351661 modified "2023-10-13" @default.
• W2149351661 title "Peptide permeases modulate transformation in<i>Streptococcus pneumoniae</i>" @default.
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• W2149351661 doi "https://doi.org/10.1111/j.1365-2958.1994.tb01076.x" @default.
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