Asset Details
Do you wish to reserve the book?
Hsp90 of E. coli modulates assembly of FtsZ, the bacterial tubulin homolog
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Hsp90 of E. coli modulates assembly of FtsZ, the bacterial tubulin homolog
Do you wish to request the book?
Hsp90 of E. coli modulates assembly of FtsZ, the bacterial tubulin homolog
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Hsp90 of E. coli modulates assembly of FtsZ, the bacterial tubulin homolog
2019
Overview
Heat shock protein 90 (Hsp90) is a highly conserved molecular chaperone involved in ATP-dependent client protein remodeling and activation. It also functions as a protein holdase, binding and stabilizing clients in an ATP-independent process. Hsp90 remodels over 300 client proteins and is essential for cell survival in eukaryotes. In bacteria, Hsp90 is a highly abundant protein, although very few clients have been identified and it is not essential for growth in many bacterial species. We previously demonstrated that in Escherichia coli, Hsp90 causes cell filamentation when expressed at high levels. Here, we have explored the cause of filamentation and identified a potentially important client of E. coli Hsp90 (Hsp90Ec), FtsZ. We observed that FtsZ, a bacterial tubulin homolog essential for cell division, fails to assemble into FtsZ rings (divisomes) in cells overexpressing Hsp90Ec. Additionally, Hsp90Ec interacts with FtsZ and inhibits polymerization of FtsZ in vitro, in an ATP-independent holding reaction. The FtsZ–Hsp90Ec interaction involves residues in the client-binding region of Hsp90Ec and in the C-terminal tail of FtsZ, where many cell-division proteins and regulators interact. We observed that E. coli deleted for the Hsp90Ec gene htpG turn over FtsZ more rapidly than wild-type cells. Additionally, the length of ΔhtpG cells is reduced compared to wild-type cells. Altogether, these results suggest that Hsp90Ec is a modulator of cell division, and imply that the polypeptide-holding function of Hsp90 may be a biologically important chaperone activity.
Publisher
National Academy of Sciences
Subject
/ Bacterial Proteins - metabolism
/ Binding
/ Clients
/ Cytoskeletal Proteins - metabolism
/ E coli
/ Escherichia coli - metabolism
/ Homology
/ HSP90 Heat-Shock Proteins - metabolism
/ HSP90 Heat-Shock Proteins - physiology
/ Kinases
/ Molecular Chaperones - metabolism
/ Molecular Chaperones - physiology
/ Proteins
/ Tubulin
