In vivo organization of the FtsZ‐ring by ZapA and ZapB revealed by quantitative super‐resolution microscopy

• DOI: 10.1111/mmi.12331
• Publication Date: 2013-07-17T07:58:37Z
• Authors: Jackson Buss; Carla Coltharp; Tao Huang; Chris Pohlmeyer; Shih‐Chin Wang; Christine Hatem; Jie Xiao
• Keywords: FtsZ

Summary In most bacterial cells, cell division is dependent on the polymerization of FtsZ protein to form a ring‐like structure ( Z ‐ring) at midcell. Despite its essential role, molecular architecture ‐ring remains elusive. this work we examine roles two ‐associated proteins, ZapA and ZapB , in assembly dynamics E scherichia coli cells. cells deleted zapA or zapB observed abnormal septa highly dynamic structures. While details these structures are difficult discern under conventional fluorescence microscopy, single‐molecule‐based super‐resolution imaging method P hotoactivated L ocalization M icroscopy PALM ) reveals that arise from disordered arrangements clusters. Quantitative analysis finds clusters larger comprise more molecules than single protofilament, likely represent distinct polymeric species inherent pathway ‐ring. Furthermore, find not due loss – MatP interaction Δ Our results suggest main function vivo may be promote association individual protofilaments but align consist multiple protofilaments.