Journal of Biological Chemistry

Krupka M, Rivas G, Rico AI, Vicente M.

The effect of two different truncations involving either the 1C domain or the simultaneous absence of the S12–13 β-strands of the FtsA protein from Streptococcus pneumoniae, located at opposite terminal sides in the molecular structure, suggests that they are essential for ATP-dependent polymerization.

These two truncated proteins are not able to polymerize themselves but can be incorporated to some extent into the FtsA⁺ polymers during the assembling process. Consequently, they block the growth of the FtsA⁺ polymers and slow down the polymerization rate. The combined action of the two truncated proteins produces an additive effect on the inhibition of FtsA⁺ polymerization, indicating that each truncation affects a different interaction site within the FtsA molecule.