دورية أكاديمية
أعرض في EDS

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

التفاصيل البيبلوغرافية
العنوان: The division protein FtsZ interacts with the small heat shock protein IbpA in Acholeplasma laidlawii.
المؤلفون: 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.
المصدر: 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.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 101731726 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1872-8006 (Electronic) Linking ISSN: 03044165 NLM ISO Abbreviation: Biochim Biophys Acta Gen Subj Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Amsterdam : Elsevier
مواضيع طبية MeSH: Heat-Shock Proteins, Small*/genetics , Heat-Shock Proteins, Small*/metabolism , Bacterial Proteins*/genetics , Bacterial Proteins*/metabolism, Acholeplasma laidlawii/genetics ; Acholeplasma laidlawii/metabolism ; Heat-Shock Response
مستخلص: 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.)
فهرسة مساهمة: Keywords: Acholeplasma laidlawii; FtsZ; IbpA; proteins interaction; sHSP
المشرفين على المادة: 0 (Heat-Shock Proteins, Small)
0 (Bacterial Proteins)
تواريخ الأحداث: Date Created: 20220807 Date Completed: 20221108 Latest Revision: 20221222
رمز التحديث: 20221222
DOI: 10.1016/j.bbagen.2022.130220
PMID: 35934107
قاعدة البيانات: MEDLINE
الوصف
تدمد:1872-8006
DOI:10.1016/j.bbagen.2022.130220