J chain is a 137-residue polypeptide that is covalently linked to polymeric immunoglobulins and participates in their synthesis and transport to external secretions. To clarify these roles, the secondary structure of J chain was characterized by computer- assisted analysis of human and mouse sequences and by circular dichroism measurements of the isolated J chain. The secondary-structure profiles obtained were very similar to those of superoxide dismutase or immunoglobulin light chain variable domains, suggesting that the J chainfolds into an eight-stranded antiparallel β-barrel and should contain approximately 37% β-sheet conformation, with the rest of the structure existing as reverse turns (random coil). The circular dichroism measurements indicated that the conformation of denatured, S-carboxymethylated or S-sulfonated J chain consists of 75% random coil and 25% β-structure. Upon reformation of disulfide bonds the percentage of β-structure in the air-oxidized J chain increased to 34%, a value that is in good agreement with the secondary-structure analysis. Two alternative models of J-chain structure, a two-domain model and a single-domain antiparallel β-sheet bilayer model (proposed in this paper), are compared.
