title: Coiled coil cytoskeletons collaborate in polar growth of Streptomyces.
abstract: Streptomyces is a multicellular mycelial bacterium, which exhibits pronounced cell polarity and grows by extension of the hyphal tips. Similarly to other polarly growing walled cells, such as filamentous fungi or pollen tubes, Streptomyces hyphae face an intrinsic problem: addition of new cell wall material causes structural weakness of the elongating tip. Cellular strategies employed by walled cells to cope with this problem are not well understood. We have identified a coiled coil protein FilP, with properties similar to those of animal intermediate filament (IF) proteins, which somehow confers rigidity and elasticity to the Streptomyces hyphae. In a recent publication we showed that FilP forms extensive cis-interconnected networks, which likely explain its biological function in determining the mechanical properties of the cells. Surprisingly, the intrinsically non-dynamic cytoskeletal network of FilP exhibits a dynamic behavior in vivo and assembles into growth-dependent polar gradients. We show that apical accumulation of FilP is dependent on its interaction with the main component of the Streptomyces polarisome, DivIVA. Thus, the same polarisome complex that orchestrates cell elongation, also recruits an additional stress-bearing structure to the growing tips with an intrinsically weak cell wall. Similar strategy might be used by all polarly growing walled cells.
authors.forename: Nora
authors.initials: N
authors.lastname: Ausmees
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D018797:Cell Cycle Proteins / Q000378:metabolism*; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D003599:Cytoskeleton / Q000378:metabolism*; D055503:Protein Multimerization / Q000502:physiology*; D048372:Streptomyces coelicolor / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D018797:Cell Cycle Proteins; D003598:Cytoskeletal Proteins