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Interactions among the early E scherichia coli divisome proteins revealed by bimolecular fluorescence complementation
Author(s) -
Pazos Manuel,
Natale Paolo,
Margolin William,
Vicente Miguel
Publication year - 2013
Publication title -
environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.954
H-Index - 188
eISSN - 1462-2920
pISSN - 1462-2912
DOI - 10.1111/1462-2920.12225
Subject(s) - ftsz , bimolecular fluorescence complementation , biology , complementation , microbiology and biotechnology , protein–protein interaction , treadmilling , cell division , protein fragment complementation assay , biophysics , cell , cytoskeleton , genetics , gene , microfilament , phenotype
Summary We used bimolecular fluorescence complementation ( BiFC ) assays to detect protein‐protein interactions of all possible pairs of the essential E scherichia coli proto‐ring components, FtsZ , FtsA and ZipA , as well as the non‐essential FtsZ ‐associated proteins ZapA and ZapB . We found an unexpected interaction between ZipA and ZapB at potential cell division sites, and when co‐overproduced, they induced long narrow constrictions at division sites that were dependent on FtsZ . These assays also uncovered an interaction between ZipA and ZapA that was mediated by FtsZ . BiFC with ZapA and ZapB showed that in addition to their expected interaction at midcell, they also interact at the cell poles. BiFC detected interaction between FtsZ and ZapB at midcell and close to the poles. Results from the remaining pairwise combinations confirmed known interactions between FtsZ and ZipA , and ZapB with itself.