AI Article Synopsis
- FtsZ is a key protein in bacterial cell division, forming a ring at midcell to coordinate division processes.
- The Thiosymbion oneisti variant of FtsZ has a unique ellipsoidal Z-ring and shows temperature sensitivity, affecting its function and leading to abnormal cell shapes when overexpressed.
- The specific structure and behavior of T. oneisti FtsZ suggest it interacts with Z-ring organizing proteins and may be adapted to the cooler environment of its nematode host.
Article Abstract
FtsZ, the bacterial tubulin-homolog, plays a central role in cell division and polymerizes into a ring-like structure at midcell to coordinate other cell division proteins. The rod-shaped gamma-proteobacterium Thiosymbion oneisti has a medial discontinuous ellipsoidal "Z-ring." T. oneisti FtsZ shows temperature-sensitive characteristics when it is expressed in , where it localizes at midcell. The overexpression of T. oneisti FtsZ interferes with cell division and results in filamentous cells. In addition, it forms ring- and barrel-like structures independently of FtsZ, which suggests that the difference in shape and size of the T. oneisti FtsZ ring is likely the result of its interaction with Z-ring organizing proteins. Similar to some temperature-sensitive alleles of FtsZ, T. oneisti FtsZ has a weak GTPase and does not polymerize in vitro. The temperature sensitivity of . Thiosymbion oneisti FtsZ is likely an adaptation to the preferred temperature of less than 30 °C of its host, the nematode
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8953583 | PMC |
| http://dx.doi.org/10.3390/ijms23063016 | DOI Listing |
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