title: Key role of two terminal domains in the bidirectional polymerization of FtsA protein.
abstract: 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.
authors.affiliation: Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Cientificas (CNB-CSIC), C/ Darwin 3, 28049 Madrid, Spain.
authors.forename: Marcin
authors.initials: M
authors.lastname: Krupka
authors.forename: Germán
authors.initials: G
authors.lastname: Rivas
authors.forename: Ana Isabel
authors.initials: AI
authors.lastname: Rico
authors.forename: Miguel
authors.initials: M
authors.lastname: Vicente
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D055503:Protein Multimerization / Q000502:physiology*; D017434:Protein Structure, Tertiary; D013296:Streptococcus pneumoniae / Q000737:chemistry / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; C065103:FtsA protein, Bacteria; D000255:Adenosine Triphosphate