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A thermosensitive defect in the ATP binding pocket of FtsA can be suppressed by allosteric changes in the dimer interface
Author(s) -
Herricks Jennifer R.,
Nguyen Diep,
Margolin William
Publication year - 2014
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12790
Subject(s) - allosteric regulation , ftsz , biology , atp hydrolysis , protein subunit , in vivo , biophysics , microbiology and biotechnology , adenosine triphosphate , dimer , biochemistry , cell division , cell , enzyme , chemistry , atpase , genetics , organic chemistry , gene
Summary In E scherichia coli , initial assembly of the Z ring for cell division requires FtsZ plus the essential Z ring‐associated proteins FtsA and ZipA . Thermosensitive mutations in ftsA , such as ftsA27 , map in or near its ATP binding pocket and result in cell division arrest at non‐permissive temperatures. We found that purified wild‐type FtsA bound and hydrolysed ATP , whereas FtsA27 was defective in both activities. FtsA27 was also less able to localize to the Z ring in vivo . To investigate the role of ATP transactions in FtsA function in vivo , we isolated intragenic suppressors of ftsA27 . Suppressor lesions in the ATP site restored the ability of FtsA27 to compete with ZipA at the Z ring, and enhanced ATP binding and hydrolysis in vitro . Notably, suppressors outside of the ATP binding site, including some mapping to the FtsA ‐ FtsA subunit interface, also enhanced ATP transactions and exhibited gain of function phenotypes in vivo . These results suggest that allosteric effects, including changes in oligomeric state, may influence the ability of FtsA to bind and/or hydrolyse ATP .