Intermolecular disulfide bonds stabilize VirB7 homodimers and VirB7/VirB9 heterodimers during biogenesis of the Agrobacterium tumefaciens T-complex transport apparatus

摘要

The Agrobacterium tumefaciens VirB7 li- poprotein contributes to the stabilization of VirB proteins during biogenesis of the putative T-complex transport appa- ratus. Here, we report that stabilization of VirB7 itself is correlated with its ability to form disulfide cross-linked homodimers via a reactive Cys-24 residue.