Tags

Type your tag names separated by a space and hit enter

The speed of FtsZ treadmilling is tightly regulated by membrane binding.
Sci Rep. 2020 Jun 26; 10(1):10447.SR

Abstract

As one of the key elements in bacterial cell division, the cytoskeletal protein FtsZ appears to be highly involved in circumferential treadmilling along the inner membrane, yielding circular vortices when transferred to flat membranes. However, it remains unclear how a membrane-targeted protein can produce these dynamics. Here, we dissect the roles of membrane binding, GTPase activity, and the unstructured C-terminal linker on the treadmilling of a chimera FtsZ protein through in vitro reconstitution of different FtsZ-YFP-mts variants on supported membranes. In summary, our results suggest substantial robustness of dynamic vortex formation, where only significant mutations, resulting in abolished membrane binding or compromised lateral interactions, are detrimental for the generation of treadmilling rings. In addition to GTPase activity, which directly affects treadmilling dynamics, we found a striking correlation of membrane binding with treadmilling speed as a result of changing the MTS on our chimera proteins. This discovery leads to the hypothesis that the in vivo existence of two alternative tether proteins for FtsZ could be a mechanism for controlling FtsZ treadmilling.

Authors+Show Affiliations

Department of Cellular and Molecular Biophysics, Max Planck Institute for Biochemistry, Martinsried, Munich, Germany. Graduate School for Quantitative Biosciences (QBM), Ludwig-Maximillians-University, Munich, Germany. Department of Engineering, Aarhus University, Aarhus, Denmark.Department of Cellular and Molecular Biophysics, Max Planck Institute for Biochemistry, Martinsried, Munich, Germany.Department of Cellular and Molecular Biophysics, Max Planck Institute for Biochemistry, Martinsried, Munich, Germany. Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), Madrid, Spain.Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), Madrid, Spain.Department of Cellular and Molecular Biophysics, Max Planck Institute for Biochemistry, Martinsried, Munich, Germany. schwille@biochem.mpg.de.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

32591587

Citation

García-Soriano, Daniela A., et al. "The Speed of FtsZ Treadmilling Is Tightly Regulated By Membrane Binding." Scientific Reports, vol. 10, no. 1, 2020, p. 10447.
García-Soriano DA, Heermann T, Raso A, et al. The speed of FtsZ treadmilling is tightly regulated by membrane binding. Sci Rep. 2020;10(1):10447.
García-Soriano, D. A., Heermann, T., Raso, A., Rivas, G., & Schwille, P. (2020). The speed of FtsZ treadmilling is tightly regulated by membrane binding. Scientific Reports, 10(1), 10447. https://doi.org/10.1038/s41598-020-67224-x
García-Soriano DA, et al. The Speed of FtsZ Treadmilling Is Tightly Regulated By Membrane Binding. Sci Rep. 2020 Jun 26;10(1):10447. PubMed PMID: 32591587.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The speed of FtsZ treadmilling is tightly regulated by membrane binding. AU - García-Soriano,Daniela A, AU - Heermann,Tamara, AU - Raso,Ana, AU - Rivas,Germán, AU - Schwille,Petra, Y1 - 2020/06/26/ PY - 2019/12/10/received PY - 2020/06/01/accepted PY - 2020/6/28/entrez PY - 2020/6/28/pubmed PY - 2020/6/28/medline SP - 10447 EP - 10447 JF - Scientific reports JO - Sci Rep VL - 10 IS - 1 N2 - As one of the key elements in bacterial cell division, the cytoskeletal protein FtsZ appears to be highly involved in circumferential treadmilling along the inner membrane, yielding circular vortices when transferred to flat membranes. However, it remains unclear how a membrane-targeted protein can produce these dynamics. Here, we dissect the roles of membrane binding, GTPase activity, and the unstructured C-terminal linker on the treadmilling of a chimera FtsZ protein through in vitro reconstitution of different FtsZ-YFP-mts variants on supported membranes. In summary, our results suggest substantial robustness of dynamic vortex formation, where only significant mutations, resulting in abolished membrane binding or compromised lateral interactions, are detrimental for the generation of treadmilling rings. In addition to GTPase activity, which directly affects treadmilling dynamics, we found a striking correlation of membrane binding with treadmilling speed as a result of changing the MTS on our chimera proteins. This discovery leads to the hypothesis that the in vivo existence of two alternative tether proteins for FtsZ could be a mechanism for controlling FtsZ treadmilling. SN - 2045-2322 UR - https://www.unboundmedicine.com/medline/citation/32591587/The_speed_of_FtsZ_treadmilling_is_tightly_regulated_by_membrane_binding L2 - http://dx.doi.org/10.1038/s41598-020-67224-x DB - PRIME DP - Unbound Medicine ER -
Try the Free App:
Prime PubMed app for iOS iPhone iPad
Prime PubMed app for Android
Prime PubMed is provided
free to individuals by:
Unbound Medicine.