Mutagenesis and chemical cross-linking suggest that Wzz dimer stability and oligomerization affect lipopolysaccharide O-antigen modal chain length control.

ABSTRACT: In Shigella flexneri, the polysaccharide copolymerase (PCP) protein Wzz(SF) confers a modal length of 10 to 17 repeat units (RUs) to the O-antigen (Oag) component of lipopolysaccharide (LPS). PCPs form oligomeric structures believed to be related to their function. To identify functionally important regions within Wzz(SF), random in-frame linker mutagenesis was used to create mutants with 5-amino-acid insertions (termed Wzz(i) proteins), and DNA sequencing was used to locate the insertions. Analysis of the resulting LPS conferred by Wzz(i) proteins identified five mutant classes. The class I mutants were inactive, resulting in nonregulated LPS Oag chains, while classes II and III conferred shorter LPS Oag chains of 2 to 10 and 8 to 14 RUs, respectively. Class IV mutants retained near-wild-

SUBMITTER: Papadopoulos M 

PROVIDER: S-EPMC2897668 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature