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Functional analysis of the cyclophilin PpiB role in bacterial cell division
Author(s) -
Skagia Aggeliki,
Zografou Chrysoula,
Venieraki Anastasia,
Fasseas Costas,
Katinakis Panagiotis,
Dimou Maria
Publication year - 2017
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/gtc.12514
Subject(s) - biology , ftsz , microbiology and biotechnology , cell division , phenotype , cell , genetics , gene
Escherichia coli PpiB is a peptidyl‐prolyl cis/trans isomerase ( PPI ase, EC : 5.2.1.8) with chaperone activity. Here, we show that the Δ ppiB deletion strain and the PpiB over‐expression wild‐type strain are both characterized by defects in cell division involving milder or severe cell filamentation, respectively. Using various PpiB mutants, we show that the PPI ase activity of PpiB is necessary for the observed cell filamentation, whereas other structural features apart from the active site are also important for this phenotype. Early divisome components zipA and ftsZ showed decreased expression in Δ ppiB cells, whereas the corresponding proteins partially suppressed the division phenotype of Δ ppiB cells as well. Although PpiB itself has no obvious specific affinity for the septal ring as a GFP translational fusion showed a diffuse cytoplasmic localization, it interacts with FtsZ employing the C‐terminal FtsZ domain, decreases its GTP ase activity and when over‐expressed shows an inhibitory effect on the proper FtsZ localization at future division sites. Furthermore, additional putative PpiB prey proteins are able to partially restore the Δ ppiB phenotype indicating that PpiB is able to control bacterial cell division by probably modulating the function of various other proteins which are indirectly associated with the process.