Biocrystallization in Bacterial and Fungal Cells and Spores
- Authors: Krupyanskii Y.F.1, Loiko N.G.1,2, Sinitsyn D.O.1, Tereshkina K.B.1, Tereshkin E.V.1, Frolov I.A.1, Chulichkov A.L.1, Bokareva D.A.2,3, Mysyakina I.S.2, Nikolaev Y.A.2, El’-Registan G.I.2, Popov V.O.2, Sokolova O.S.4, Shaitan K.V.4, Popov A.N.5
-
Affiliations:
- Semenov Institute of Chemical Physics
- Federal Research Centre “Fundamentals of Biotechnology,”
- National Research Centre “Kurchatov Institute,”
- Moscow State University
- European Synchrotron Radiation Facility
- Issue: Vol 63, No 4 (2018)
- Pages: 594-599
- Section: Structure of Macromolecular Compounds
- URL: https://journals.rcsi.science/1063-7745/article/view/192695
- DOI: https://doi.org/10.1134/S1063774518040144
- ID: 192695
Cite item
Abstract
A series of X-ray diffraction experiments were performed for the first time to study stress-induced biocrystallization (structural response to stress) in the bacteria E. coli, the spore-forming bacteria Bacillus cereus, and in cells and spores of the mycelial fungus Umbelopsis ramanniana. High-intensity areas with spacings of 90 and 44 Å are indicative of a periodically ordered arrangement (most likely nanocrystalline) of the bacterial nucleoid. For the starved bacteria Bacillus cereus, a peak at a spacing of 45 Å is also assigned to nanocrystalline complexes of DNA with the Dps protein. The spores of the fungus Umbelopsis ramanniana VKM F-582, as well as the spores of Bacillus cereus, form ordered arrays of DNA molecules with DNA-condensing acid-soluble proteins SASPs. Starved dehydrated mycelial cells of the fungus Umbelopsis ramanniana form ordered structures with spacings from 27 to 55 Å. A series of peaks reflect the formation of a number of ordered protein arrays, apparently with DNA, with continuously varying characteristic interplanar spacings.
About the authors
Y. F. Krupyanskii
Semenov Institute of Chemical Physics
Author for correspondence.
Email: yufk@chph.ras.ru
Russian Federation, Moscow, 117977
N. G. Loiko
Semenov Institute of Chemical Physics; Federal Research Centre “Fundamentals of Biotechnology,”
Email: yufk@chph.ras.ru
Russian Federation, Moscow, 117977; Moscow, 119071
D. O. Sinitsyn
Semenov Institute of Chemical Physics
Email: yufk@chph.ras.ru
Russian Federation, Moscow, 117977
K. B. Tereshkina
Semenov Institute of Chemical Physics
Email: yufk@chph.ras.ru
Russian Federation, Moscow, 117977
E. V. Tereshkin
Semenov Institute of Chemical Physics
Email: yufk@chph.ras.ru
Russian Federation, Moscow, 117977
I. A. Frolov
Semenov Institute of Chemical Physics
Email: yufk@chph.ras.ru
Russian Federation, Moscow, 117977
A. L. Chulichkov
Semenov Institute of Chemical Physics
Email: yufk@chph.ras.ru
Russian Federation, Moscow, 117977
D. A. Bokareva
Federal Research Centre “Fundamentals of Biotechnology,”; National Research Centre “Kurchatov Institute,”
Email: yufk@chph.ras.ru
Russian Federation, Moscow, 119071; Moscow, 123098
I. S. Mysyakina
Federal Research Centre “Fundamentals of Biotechnology,”
Email: yufk@chph.ras.ru
Russian Federation, Moscow, 119071
Y. A. Nikolaev
Federal Research Centre “Fundamentals of Biotechnology,”
Email: yufk@chph.ras.ru
Russian Federation, Moscow, 119071
G. I. El’-Registan
Federal Research Centre “Fundamentals of Biotechnology,”
Email: yufk@chph.ras.ru
Russian Federation, Moscow, 119071
V. O. Popov
Federal Research Centre “Fundamentals of Biotechnology,”
Email: yufk@chph.ras.ru
Russian Federation, Moscow, 119071
O. S. Sokolova
Moscow State University
Email: yufk@chph.ras.ru
Russian Federation, Moscow, 119991
K. V. Shaitan
Moscow State University
Email: yufk@chph.ras.ru
Russian Federation, Moscow, 119991
A. N. Popov
European Synchrotron Radiation Facility
Email: yufk@chph.ras.ru
France, Grenoble, 38000