The division protein FtsZ interacts with the small heat shock protein IbpA in Acholeplasma laidlawii.

Autor: Chernova LS; Kazan Federal University, 18 Kremlevskaya street, 420008 Kazan, Russia; Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky ave., 194064 St. Petersburg, Russia., Vedyaykin AD; Peter the Great St. Petersburg Polytechnic University, 29 Polytechnicheskaya street, 195251 St. Petersburg, Russia., Bogachev MI; St. Petersburg Electrotechnical University, 5 Professor Popov street, 197376 St. Petersburg, Russia., Fedorova MS; Kazan Federal University, 18 Kremlevskaya street, 420008 Kazan, Russia., Ivanov VA; Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky ave., 194064 St. Petersburg, Russia., Vishnyakov IE; Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky ave., 194064 St. Petersburg, Russia. Electronic address: innvish@incras.ru., Kayumov AR; Kazan Federal University, 18 Kremlevskaya street, 420008 Kazan, Russia. Electronic address: kairatr@yandex.ru.
Jazyk: angličtina
Zdroj: Biochimica et biophysica acta. General subjects [Biochim Biophys Acta Gen Subj] 2022 Dec; Vol. 1866 (12), pp. 130220. Date of Electronic Publication: 2022 Aug 05.
DOI: 10.1016/j.bbagen.2022.130220
Abstrakt: Small heat shock proteins (sHSPs) control the proteins stability in the cell preventing their irreversible denaturation. While many mycoplasmas possess the sHSP gene in the genome, Acholeplasma laidlawii is the only mycoplasma capable of surviving in the environment. Here we report that the sHSP IbpA directly interacts with the key division protein FtsZ in A. laidlawii, representing the first example of such interaction in prokaryotes. FtsZ co-immunoprecipitates with IbpA from A. laidlawii crude extract and in vitro binds IbpA with K D  ~ 1 μM. Proteins co-localize in the soluble fraction of the cell at 30-37 °C and in the non-soluble fraction after 1 h exposition to cold stress (4 °C). Under heat shock conditions (42 °C) the amount of FtsZ decreases and the protein remains in both soluble and non-soluble fractions. Furthermore, in vitro, FtsZ co-elutes with IbpA His6 from A. laidlawii crude extract at any temperatures from 4 to 42 °C, with highest yield at 42 °C. Moreover, in vitro FtsZ retains its GTPase activity in presence of IbpA, and the filaments and bundles formation seems to be even improved by sHSP at 30-37 °C. At extreme temperatures, either 4 or 42 °C, IbpA facilitates FtsZ polymerization, although filaments under 4 °C appears shorter and with lower density, while at 42 °C IbpA sticks around the bundles, preventing their destruction by heat. Taken together, these data suggest that sHSP IbpA in A. laidlawii contributes to the FtsZ stability control and may be assisting appropriate cell division under unfavorable conditions.
Competing Interests: Declaration of Competing Interest The authors declare no conflict of interest.
(Copyright © 2022 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
Externí odkaz: