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- W2788382186 endingPage "235" @default.
- W2788382186 startingPage "235" @default.
- W2788382186 abstract "<ns4:p>To generate two cells from one, bacteria such as<ns4:italic>Escherichia coli</ns4:italic>use a complex of membrane-embedded proteins called the divisome that synthesize the division septum. The initial stage of cytokinesis requires a tubulin homolog, FtsZ, which forms polymers that treadmill around the cell circumference. The attachment of these polymers to the cytoplasmic membrane requires an actin homolog, FtsA, which also forms dynamic polymers that directly bind to FtsZ. Recent evidence indicates that FtsA and FtsZ regulate each other’s oligomeric state in<ns4:italic>E. coli</ns4:italic>to control the progression of cytokinesis, including the recruitment of septum synthesis proteins. In this review, we focus on recent advances in our understanding of protein-protein association between FtsZ and FtsA in the initial stages of divisome function, mainly in the well-characterized<ns4:italic>E. coli</ns4:italic>system.</ns4:p>" @default.
- W2788382186 created "2018-03-06" @default.
- W2788382186 creator A5011693234 @default.
- W2788382186 creator A5022252728 @default.
- W2788382186 date "2018-02-28" @default.
- W2788382186 modified "2023-09-30" @default.
- W2788382186 title "Unite to divide: Oligomerization of tubulin and actin homologs regulates initiation of bacterial cell division" @default.
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