Abstract
Similar to its eukaryotic counterpart, the prokaryotic cytoskeleton is essential for the structural and mechanical properties of bacterial cells. The essential protein FtsZ is a central player in the cytoskeletal family, forms a cytokinetic ring at mid-cell, and recruits the division machinery to orchestrate cell division. Cells depleted of or lacking functional FtsZ do not divide and grow into long filaments that eventually lyse. FtsZ has been studied extensively as a target for antibacterial development. In this Perspective, we review the structural and biochemical properties of FtsZ, its role in cell biochemistry and physiology, the different mechanisms of inhibiting FtsZ, small molecule antagonists (including some misconceptions about mechanisms of action), and their discovery strategies. This collective information will inform chemists on different aspects of FtsZ that can be (and have been) used to develop successful strategies for devising new families of cell division inhibitors.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 6975-6998 |
| Number of pages | 24 |
| Journal | Journal of Medicinal Chemistry |
| Volume | 59 |
| Issue number | 15 |
| DOIs | |
| State | Published - Aug 11 2016 |
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ASJC Scopus subject areas
- Molecular Medicine
- Drug Discovery
Cite this
Targeting the Bacterial Division Protein FtsZ. / Hurley, Katherine A.; Santos, Thiago M A; Nepomuceno, Gabriella M.; Huynh, Valerie; Shaw, Jared T.; Weibel, Douglas B.
In: Journal of Medicinal Chemistry, Vol. 59, No. 15, 11.08.2016, p. 6975-6998.Research output: Contribution to journal › Review article
}
TY - JOUR
T1 - Targeting the Bacterial Division Protein FtsZ
AU - Hurley, Katherine A.
AU - Santos, Thiago M A
AU - Nepomuceno, Gabriella M.
AU - Huynh, Valerie
AU - Shaw, Jared T.
AU - Weibel, Douglas B.
PY - 2016/8/11
Y1 - 2016/8/11
N2 - Similar to its eukaryotic counterpart, the prokaryotic cytoskeleton is essential for the structural and mechanical properties of bacterial cells. The essential protein FtsZ is a central player in the cytoskeletal family, forms a cytokinetic ring at mid-cell, and recruits the division machinery to orchestrate cell division. Cells depleted of or lacking functional FtsZ do not divide and grow into long filaments that eventually lyse. FtsZ has been studied extensively as a target for antibacterial development. In this Perspective, we review the structural and biochemical properties of FtsZ, its role in cell biochemistry and physiology, the different mechanisms of inhibiting FtsZ, small molecule antagonists (including some misconceptions about mechanisms of action), and their discovery strategies. This collective information will inform chemists on different aspects of FtsZ that can be (and have been) used to develop successful strategies for devising new families of cell division inhibitors.
AB - Similar to its eukaryotic counterpart, the prokaryotic cytoskeleton is essential for the structural and mechanical properties of bacterial cells. The essential protein FtsZ is a central player in the cytoskeletal family, forms a cytokinetic ring at mid-cell, and recruits the division machinery to orchestrate cell division. Cells depleted of or lacking functional FtsZ do not divide and grow into long filaments that eventually lyse. FtsZ has been studied extensively as a target for antibacterial development. In this Perspective, we review the structural and biochemical properties of FtsZ, its role in cell biochemistry and physiology, the different mechanisms of inhibiting FtsZ, small molecule antagonists (including some misconceptions about mechanisms of action), and their discovery strategies. This collective information will inform chemists on different aspects of FtsZ that can be (and have been) used to develop successful strategies for devising new families of cell division inhibitors.
UR - http://www.scopus.com/inward/record.url?scp=84980327998&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84980327998&partnerID=8YFLogxK
U2 - 10.1021/acs.jmedchem.5b01098
DO - 10.1021/acs.jmedchem.5b01098
M3 - Review article
VL - 59
SP - 6975
EP - 6998
JO - Journal of Medicinal Chemistry
JF - Journal of Medicinal Chemistry
SN - 0022-2623
IS - 15
ER -