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Bacterial Luciferases from Vibrio harveyi and Photobacterium leiognathi Demonstrate Different Conformational Stability as Detected by Time-Resolved Fluorescence Spectroscopy.

التفاصيل البيبلوغرافية
العنوان: Bacterial Luciferases from Vibrio harveyi and Photobacterium leiognathi Demonstrate Different Conformational Stability as Detected by Time-Resolved Fluorescence Spectroscopy.
المؤلفون: Nemtseva EV; Siberian Federal University, 660041 Krasnoyarsk, Russia.; Photobiology Laboratory, Institute of Biophysics SB RAS, 660036 Krasnoyarsk, Russia., Gulnov DV; Siberian Federal University, 660041 Krasnoyarsk, Russia., Gerasimova MA; Siberian Federal University, 660041 Krasnoyarsk, Russia., Sukovatyi LA; Siberian Federal University, 660041 Krasnoyarsk, Russia., Burakova LP; Siberian Federal University, 660041 Krasnoyarsk, Russia.; Photobiology Laboratory, Institute of Biophysics SB RAS, 660036 Krasnoyarsk, Russia., Karuzina NE; Siberian Federal University, 660041 Krasnoyarsk, Russia., Melnik BS; Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia., Kratasyuk VA; Siberian Federal University, 660041 Krasnoyarsk, Russia.; Photobiology Laboratory, Institute of Biophysics SB RAS, 660036 Krasnoyarsk, Russia.
المصدر: International journal of molecular sciences [Int J Mol Sci] 2021 Sep 28; Vol. 22 (19). Date of Electronic Publication: 2021 Sep 28.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: MDPI Country of Publication: Switzerland NLM ID: 101092791 Publication Model: Electronic Cited Medium: Internet ISSN: 1422-0067 (Electronic) Linking ISSN: 14220067 NLM ISO Abbreviation: Int J Mol Sci Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Basel, Switzerland : MDPI, [2000-
مواضيع طبية MeSH: Molecular Dynamics Simulation*, Luciferases, Bacterial/*chemistry , Photobacterium/*chemistry , Vibrio/*chemistry, Protein Domains ; Spectrometry, Fluorescence
مستخلص: Detecting the folding/unfolding pathways of biological macromolecules is one of the urgent problems of molecular biophysics. The unfolding of bacterial luciferase from Vibrio harveyi is well-studied, unlike that of Photobacterium leiognathi , despite the fact that both of them are actively used as a reporter system. The aim of this study was to compare the conformational transitions of these luciferases from two different protein subfamilies during equilibrium unfolding with urea. Intrinsic steady-state and time-resolved fluorescence spectra and circular dichroism spectra were used to determine the stages of the protein unfolding. Molecular dynamics methods were applied to find the differences in the surroundings of tryptophans in both luciferases. We found that the unfolding pathway is the same for the studied luciferases. However, the results obtained indicate more stable tertiary and secondary structures of P. leiognathi luciferase as compared to enzyme from V. harveyi during the last stage of denaturation, including the unfolding of individual subunits. The distinctions in fluorescence of the two proteins are associated with differences in the structure of the C-terminal domain of α-subunits, which causes different quenching of tryptophan emissions. The time-resolved fluorescence technique proved to be a more effective method for studying protein unfolding than steady-state methods.
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معلومات مُعتمدة: FSRZ-2020-0006 Ministry of Science and Higher Education of the Russian Federation; 20-34-90118 Russian Foundation for Basic Research; 20-44-243002 RFBR and Krasnoyarsk Territory and Krasnoyarsk Regional Fund of Science; 20-44-240006 RFBR and Krasnoyarsk Territory and Krasnoyarsk Regional Fund of Science
فهرسة مساهمة: Keywords: FRET; bacterial luciferase; conformational stability; molecular dynamics; time-resolved spectroscopy; tryptophan fluorescence; unfolding pathway; urea-induced denaturation
المشرفين على المادة: EC 1.14.14.3 (Luciferases, Bacterial)
SCR Organism: Photobacterium leiognathi; Vibrio harveyi
تواريخ الأحداث: Date Created: 20211013 Date Completed: 20211027 Latest Revision: 20211027
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC8508739
DOI: 10.3390/ijms221910449
PMID: 34638798
قاعدة البيانات: MEDLINE
الوصف
تدمد:1422-0067
DOI:10.3390/ijms221910449