Tanya V. Ivashina

G. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms

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ВН

В. Н. Ксензенко

Institute of Protein Research

Marina V. Donova

G. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms

Dmitry V. Dovbnya

G. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms

Leonid M. Vinokurov

Institute of Bioorganic Chemistry

Victor Marchenkov

Institute of Protein Research

Victoria V. Zherdeva

A N Bach Institute of Biochemistry

Eugeny Y. Bragin

G. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms

Alexander P. Savitsky

A N Bach Institute of Biochemistry

Victoria Shtratnikova

Lomonosov Moscow State University

Alexander Kanapin

Peter the Great St. Petersburg Polytechnic University

Cooperative Institutions

Russian Academy of Sciences

G. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms

Lomonosov Moscow State University

Institute of Bioorganic Chemistry

A N Bach Institute of Biochemistry

Institute of Protein Research

Moscow State University

Federal Center Research Fundamentals of Biotechnology

Pushchino State Institute of Natural Sciences

Institute of Business and Law

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Draft Genome Sequence of Mycolicibacterium smegmatis VKM Ac-1171 Contains Full Set of Sterol Catabolic Genes

Microbiology Resource Announcements (2022)

Dmitry V. Dovbnya Eugeny Y. Bragin Tanya V. Ivashina Marina V. Donova

Mycolicibacterium smegmatis VKM Ac-1171 is a saprotrophic bacterium that was isolated several decades ago and is deposited in microbial collections around the world. We report here a draft genome sequence of the strain. Annotation of the genome revealed the presence of a complete set of genes related to the sterol catabolic pathway.

Catabolism

Strain (injury)

Sequence (biology)

10.1128/mra.00772-22

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Citations (2)

[The dependence of stability of the green fluorescent protein-obelin hybrids on the nature of their constituent modules and the structure of the amino acid linker].

Russian Journal of Bioorganic Chemistry (2001)

Vitaly S. Skosyrev A. Yu. Gorokhovatsky Leonid M. Vinokurov Н. В. Руденко Tanya V. Ivashina

Aequorea victoria

Photoprotein

Proteolysis

10.1023/a:1012344414924

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Citations (3)

Monomerization of the photoconvertible fluorescent protein SAASoti by rational mutagenesis of single amino acids

Scientific Reports (2018)

Ilya D. Solovyev Alexandra V. Gavshina Aditya Katti Alexey I. Chizhik Leonid M. Vinokurov

Photoconvertible fluorescent proteins (PCFPs) are widely used as markers for the visualization of intracellular processes and for sub-diffraction single-molecule localization microscopy. Although wild type of a new photoconvertible fluorescent protein SAASoti tends to aggregate, we succeeded, via rational mutagenesis, to obtain variants that formed either tetramers or monomers. We compare two approaches: one is based on the structural similarity between SAASoti and Kaede, which helped us to identify a single point mutation (V127T) at the protein's hydrophobic interface that leads to monomerization. The other is based on a chemical modification of amino groups of SAASoti with succinic anhydride, which converts the protein aggregates into monomers. Mass-spectrometric analysis helped us to identify that the modification of a single ε-amino group of lysine K145 in the strongly charged interface AB was sufficient to convert the protein into its tetrameric form. Furthermore, site-directed mutagenesis was used to generate mutants that proved to be either monomeric or tetrameric, both capable of rapid green-to-red photoconversion. This allows SAASoti to be used as a photoconvertible fluorescent marker for in vivo cell studies.

Rational design

Succinic anhydride

10.1038/s41598-018-33250-z

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Citations (12)

[Structure-functional organization of exopolysaccharide biosynthetic genes in Rhizobium leguminosarum bv. viciae VF39].

PubMed (1999)

Sadykov Mr Tanya V. Ivashina Alexander Kanapin Shliapnikov Mg Ksenzenko Vn

Rhizobium leguminosarum

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Citations (22)

Comparison of the substrate specificity of two ring-hydroxylating dioxygenases from Sphingomonas sp. VKM B-2434 to polycyclic aromatic hydrocarbons

Biodegradation (2014)

M. A. Baboshin Tanya V. Ivashina Chernykh Am L. A. Golovleva

Fluoranthene

Dioxygenase

Sphingomonas

10.1007/s10532-014-9692-3

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Citations (4)

Mutation in the pssM gene encoding ketal pyruvate transferase leads to disruption of Rhizobium leguminosarum bv. viciae – Pisum sativum symbiosis*

Journal of Applied Microbiology (2010)

Tanya V. Ivashina Elena Fedorova N.P. Ashina N. A. Kalinchuk Т. Н. Дружинина

Aims: To study the question whether acidic exopolysaccharide (EPS) modification, e.g. pyruvylation, plays any role in the development of Rhizobium leguminosarum/Pisum sativum symbiosis. Method and Results: The amino acid sequence deduced from the pssM gene, localized within the pss (polysaccharide synthesis) gene locus, was shown to be homologous to several known and putative ketal pyruvate transferases, including ExoV from Sinorhizobium meliloti and GumL from Xanthomonas campestris. Rh. l. bv. viciae strain VF39 carrying a Km-cassette insertion into the pssM gene was obtained by the gene replacement technique. Knock-out of pssM led to the absence of the pyruvic acid ketal group at the subterminal glucose in the repeating unit of EPS as it was shown by 13C and 1H nuclear magnetic resonance (NMR) analysis. Complementation in trans restored the EPS modification in the pssM mutant. Disruption of the pssM gene resulted also in the formation of aberrant non-nitrogen-fixing nodules on peas. Ultrastructural studies of mutant nodules revealed normal nodule invasion and release of bacteria into the plant cell cytoplasm, but further differentiation of bacteroids was impaired, and the existing symbiosomes underwent lysis. Conclusion: PssM encodes ketal pyruvate transferase involved in the modification of the Rh. l. bv. viciae EPS. The absence of subterminal glucose pyruvylation in the EPS repeating units negatively influences (directly or indirectly) the formation of the nitrogen-fixing symbiosis with peas. Significance and Impact of the Study: Our finding that the absence of modification even at the single position of EPS is likely to be crucial for establishment of nitrogen-fixing symbiosis argues in favour of the idea concerning their specific signalling role in this process.

Rhizobium leguminosarum

Sinorhizobium meliloti

10.1111/j.1365-2672.2010.04702.x

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Citations (30)

Back to GroEL-Assisted Protein Folding: GroES Binding-Induced Displacement of Denatured Proteins from GroEL to Bulk Solution

Biomolecules (2020)

Victor Marchenkov Andrey Yu. Gorokhovatsky Natalia Marchenko Tanya V. Ivashina Gennady V. Semisotnov

The main events in chaperone-assisted protein folding are the binding and ligand-induced release of substrate proteins. Here, we studied the location of denatured proteins previously bound to the GroEL chaperonin resulting from the action of the GroES co-chaperonin in the presence of Mg-ATP. Fluorescein-labeled denatured proteins (α-lactalbumin, lysozyme, serum albumin, and pepsin in the presence of thiol reagents at neutral pH, as well as an early refolding intermediate of malate dehydrogenase) were used to reveal the effect of GroES on their interaction with GroEL. Native electrophoresis has demonstrated that these proteins tend to be released from the GroEL-GroES complex. With the use of biotin- and fluorescein-labeled denatured proteins and streptavidin fused with luciferase aequorin (the so-called streptavidin trap), the presence of denatured proteins in bulk solution after GroES and Mg-ATP addition has been confirmed. The time of GroES-induced dissociation of a denatured protein from the GroEL surface was estimated using the stopped-flow technique and found to be much shorter than the proposed time of the GroEL ATPase cycle.

GroES

Chaperonin

Foldase

Chaperone (clinical)

10.3390/biom10010162

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Citations (10)

Mutation L232H Promotes Chromophore Maturation of EGFP-Based Fluorescent Fusion Proteins

Crystallography Reports (2018)

A. A. Simanovskaya Tanya V. Ivashina Yu. S. Zeifman T. V. Fateeva M. V. Krukova

Chromophore

Fluorescent protein