Extended Data Figure 8 : Analysis of MapZ in vivo phosphorylation and impact on FtsZ GTPase activity and polymerization.

From: MapZ marks the division sites and positions FtsZ rings in Streptococcus pneumoniae

Extended Data Figure 8

a, b, MapZ is phosphorylated on threonine 67 (a) and threonine 78 (b). The spectra show the fragmentation pattern of the phosphopeptides DEIEADKFAT(ph)R corresponding to amino acids 58–68 and KEEFVET(ph)QSLDDLIQEM(ox)R corresponding to amino acids 72–89. c, Influence of MapZ and MapZ-2TE cytoplasmic domains on FtsZ GTPase activity. Purified FtsZ was incubated with GTP either alone or in the presence of MapZ or MapZ-2TE cytoplasmic domains and free phosphate was revealed using malachite green colour development. Data are shown with s.d. for three independent experiments. d, FtsZ polymerization in the presence of MapZcyto, wild-type or mutated, cytoplasmic domains. FtsZ was incubated in the presence or absence of GTP and either MapZ or MapZ-2TE. The samples were then processed as described in Methods. Images are representative of experiments made in triplicate.