Cytological and biochemical characterization of the FtsA cell division protein of Bacillus subtilis.

Abstract:

:The actin-like protein FtsA is present in many eubacteria, and genetic experiments have shown that it plays an important, sometimes essential, role in cell division. Here, we show that Bacillus subtilis FtsA is targeted to division sites in both vegetative and sporulating cells. As in other organisms FtsA is probably recruited immediately after FtsZ. In sporulating cells of B. subtilis FtsZ is recruited to potential division sites at both poles of the cell, but asymmetric division occurs at only one pole. We have now found that FtsA is recruited to only one cell pole, suggesting that it may play an important role in the generation of asymmetry in this system. FtsA is present in much higher quantities in B. subtilis than in Escherichia coli, with approximately one molecule of FtsA for five of FtsZ. This means that there is sufficient FtsA to form a complete circumferential ring at the division site. Therefore, FtsA may have a direct structural role in cell division. We have purified FtsA and shown that it behaves as a dimer and that it has both ATP-binding and ATP-hydrolysis activities. This suggests that ATP hydrolysis by FtsA is required, together with GTP hydrolysis by FtsZ, for cell division in B. subtilis (and possibly in most eubacteria).

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Feucht A,Lucet I,Yudkin MD,Errington J

doi

10.1046/j.1365-2958.2001.02356.x

subject

Has Abstract

pub_date

2001-04-01 00:00:00

pages

115-25

issue

1

eissn

0950-382X

issn

1365-2958

pii

mmi2356

journal_volume

40

pub_type

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