Abstract:
:DivIB, DivIC and FtsL are bacterial proteins essential for cell division, which show interdependencies for their stabilities and localization. We have reconstituted in vitro a trimeric complex consisting of the recombinant extracellular domains of the three proteins from Streptococcus pneumoniae. The extracellular domain of DivIB was found to associate with a heterodimer of those of DivIC and FtsL. The heterodimerization of DivIC and FtsL was artificially constrained by fusion with interacting coiled-coils. Immunofluorescence experiments showed that DivIC is always localized at mid-cell, in contrast to DivIB and FtsL, which are co-localized with DivIC only during septation. Taken together, our data suggest that assembly of the trimeric complex DivIB/DivIC/FtsL is regulated during the cell cycle through controlled formation of the DivIC/FtsL heterodimer.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Noirclerc-Savoye M,Le Gouëllec A,Morlot C,Dideberg O,Vernet T,Zapun Adoi
10.1111/j.1365-2958.2004.04408.xsubject
Has Abstractpub_date
2005-01-01 00:00:00pages
413-24issue
2eissn
0950-382Xissn
1365-2958pii
MMI4408journal_volume
55pub_type
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