title: Characterization of the Synechocystis strain PCC 6803 penicillin-binding proteins and cytokinetic proteins FtsQ and FtsW and their network of interactions with ZipN.
abstract: Because very little is known about cell division in noncylindrical bacteria and cyanobacteria, we investigated 10 putative cytokinetic proteins in the unicellular spherical cyanobacterium Synechocystis strain PCC 6803. Concerning the eight penicillin-binding proteins (PBPs), which define three classes, we found that Synechocystis can survive in the absence of one but not two PBPs of either class A or class C, whereas the unique class B PBP (also termed FtsI) is indispensable. Furthermore, we showed that all three classes of PBPs are required for normal cell size. Similarly, the putative FtsQ and FtsW proteins appeared to be required for viability and normal cell size. We also used a suitable bacterial two-hybrid system to characterize the interaction web among the eight PBPs, FtsQ, and FtsW, as well as ZipN, the crucial FtsZ partner that occurs only in cyanobacteria and plant chloroplasts. We showed that FtsI, FtsQ, and ZipN are self-interacting proteins and that both FtsI and FtsQ interact with class A PBPs, as well as with ZipN. Collectively, these findings indicate that ZipN, in interacting with FtsZ and both FtsI and FtQ, plays a similar role to the Escherichia coli FtsA protein, which is missing in cyanobacteria and chloroplasts.
authors: CEA, iBiTec-S SBIGeM LBI, Bat. 142, CEA Saclay F-91191, Gif sur Yvette CEDEX 91191, France.
authors: Martial
authors: M
authors: Marbouty
authors: Khalil
authors: K
authors: Mazouni
authors: Cyril
authors: C
authors: Saguez
authors: Corinne
authors: C
authors: Cassier-Chauvat
authors: Franck
authors: F
authors: Chauvat
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D005434:Flow Cytometry; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D008954:Models, Biological; D009154:Mutation; D046915:Penicillin-Binding Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D011485:Protein Binding / Q000235:genetics / Q000502:physiology; D046939:Synechocystis / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D020798:Two-Hybrid System Techniques
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins; D046915:Penicillin-Binding Proteins; C061684:FtsW protein, Bacteria