A bacterial actin with high ATPase activity regulates the polymerization of a partner MreB isoform essential for Spiroplasma swimming motility.

ABSTRACT: Spiroplasma is a wall-less helical bacterium that is characterized by a unique swimming motility involving five isoforms of the bacterial actin MreBs (SMreB1-5). The functions of SMreBs are unique in the MreB family proteins, as their counterparts in walled bacteria localize the cell wall synthesis complex by forming filaments that slowly turn over to maintain the cell shape. In vitro analyses of individual SMreBs provide clues to understand the detailed molecular mechanism of Spiroplasma swimming. However, the purification difficulties have hampered in vitro analyses of one of the SMreBs, SMreB1, which is essential for the swimming. Here, we isolated soluble SMreB1 of Spiroplasma eriocheiris (SpeMreB1) and evaluated its activity. SpeMreB1 was expressed as a fusion with a solubilization ta

SUBMITTER: Takahashi D 

PROVIDER: S-EPMC12337190 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature