Our mBio paper reporting a new interaction between the essential divisome proteins ZipA and FtsZ, featuring Dr. Todd Cameron as first author, is out:
For the last 20 years it has been assumed that the only interaction between FtsZ and one of its two essential membrane anchors, ZipA, was through the C-terminal conserved peptide of FtsZ. This peptide also interacts with FtsZ's other key membrane anchor, FtsA, and it is likely that FtsA and ZipA compete for binding to this small peptide. However, our new findings show the C-terminal region is completely dispensible for this novel interaction with ZipA, which occurs on the opposite face of ZipA's globular domain. We conclude that FtsZ interacts with ZipA both via its C-terminal peptide (part 2 in Figure) and its core domain (part 3 in Figure). Mutants in the novel domain of ZipA involved in binding the FtsZ core show defects in cell division, indicating that the novel interaction has an important cell division function. We are currently working on understanding what that function might be.