M. G. Shlyapnikov

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

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В. Н. Ксензенко

Institute of Protein Research

Alexander S. Solonin

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

Igor Granovsky

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

Sergey G. Mayorov

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

Marina V. Zakharova

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

A.A. Bayev

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

Valentine M. Kryukov

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

Ekaterina A. Rodikova

St Petersburg University

M. A. Nesmeyanova

Voronezh State Agrarian University named after Emperor Peter the Great

Zhanna I. Budarina

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

Cooperative Institutions

Russian Academy of Sciences

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

Institute of Protein Research

Institute of Bioorganic Chemistry

Pushchino State Institute of Natural Sciences

Queen's University Belfast

Rutgers, The State University of New Jersey

Lomonosov Moscow State University

Engelhardt Institute of Molecular Biology

Kurchatov Institute

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A new Bacillus cereus DNA-binding protein, HlyIIR, negatively regulates expression of B. cereus haemolysin II

Microbiology (2004)

Zhanna I. Budarina Dmitri Nikitin Nikolay Zenkin Marina V. Zakharova Ekaterina Semenova

Haemolysin II, HlyII, is one of several cytotoxic proteins produced by Bacillus cereus, an opportunistic human pathogen that causes food poisoning. The hlyII gene confers haemolytic activity to Escherichia coli cells. Here a new B. cereus gene, hlyIIR, which is located immediately downstream of hlyII and regulates hlyII expression, is reported. The deduced amino acid sequence of HlyIIR is similar to prokaryotic DNA-binding transcriptional regulators of the TetR/AcrA family. Measurements of haemolytic activity levels and of hlyII promoter activity levels using gene fusions and primer-extension assays demonstrated that, in E. coli, hlyII transcription decreased in the presence of hlyIIR. Recombinant HlyIIR binds to a 22 bp inverted DNA repeat centred 48 bp upstream of the hlyII promoter transcription initiation point. In vitro transcription studies showed that HlyIIR inhibits transcription from the hlyII promoter by binding to the 22 bp repeat and RNA polymerase, and by decreasing the formation of the catalytically competent open promoter complex.

Transcription

Cereus

Terminator (solar)

TetR

10.1099/mic.0.27142-0

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Citations (44)

POWER ANALYSIS OF THE MARKER CONTROL MECHANISM GRAIN DRILLS SUBM-3,6

Современные наукоемкие технологии (Modern High Technologies) (2019)

Vladimir F. Kupryashkin M. G. Shlyapnikov Andrey V. Bezrukov Aleksey S. Knyazkov Vladimir V. Kupryashkin

СИЛоВоЙ аНаЛИЗ МеХаНИЗМа УПРаВЛеНИЯМаРКеРоМ ЗеРНоВоЙ СеЯЛКИ СУБМ-3,6Купряшкин В.Ф., Шляпников М

10.17513/snt.37836

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A Method for Producing Protease Ps273r of the African Swine Fever Virus

Igor Granovsky Danil S. Kalinin Sergey G. Mayorov Marina Yu. Zemskova О. Р. Латыпов

African Swine Fever

10.2139/ssrn.4879833

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New Site-Specific Endonucleases F-TflI, F-TflII, and F-TflIV Encoded by Bacteriophage T5

Molecular Biology (2004)

Natalia Akulenko Tanya V. Ivashina Lyubov Shaloiko M. G. Shlyapnikov В. Н. Ксензенко

Recognition sequence

Palindromic sequence

10.1023/b:mbil.0000037005.52556.0f

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Citations (7)

Complete nucleotide sequence of the Hsd plasmid pECO29 and identification of its functional regions

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression (1998)

Marina V. Zakharova Alexander V Pertzev Anatoly N. Kravetz Irina V. Beletskaya M. G. Shlyapnikov

T-DNA Binary system

Inverted repeat

10.1016/s0167-4781(98)00051-7

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Citations (9)

A phage T4 site‐specific endonuclease, SegE, is responsible for a non‐reciprocal genetic exchange between T‐even‐related phages

FEBS Letters (1997)

Farid A. Kadyrov M. G. Shlyapnikov Valentine M. Kryukov

The bacteriophage T4 seg E gene encoding site‐specific endonuclease lies between the hoc .1 and uvs W genes. The similar region of T‐even‐related phage RB30 lacks the seg E gene. Here we demonstrate that the phage T4 seg E gene is inherited preferably by progeny of mixed infection with RB30. The preferred inheritance of the seg E gene depends on its own expression and is based on a non‐reciprocal homologous recombination event providing the transfer of the gene from the seg E‐containing to the seg E‐lacking allele. The SegE endonuclease cleaves DNA in a site located at the 5′ end of the uvs W gene in the RB30 genome. The T4 DNA is also cleaved by the enzyme, but less efficiently. The cleavage at the RB30 site appears to initiate the observed conversion, which is stimulated by DNA homology and accompanied by co‐conversion of flanking markers. Our findings provide a novel example of endonuclease‐dependent generation of genetic variation in prokaryotes.

Homing endonuclease

10.1016/s0014-5793(97)01098-3

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Citations (30)

The study of biogenesis and secretion of alkaline phoshatase and its mutant forms in Escherichia coli. III. Substitutions of N-terminal amino acid of alkaline phosphatase affect its biogenesis

Molekulyarnaya Biologiya (1994)

A. L. Karamyshev Andrey E. Kalinin Michael Khmelnitsky M. G. Shlyapnikov В. Н. Ксензенко

Source

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Transfer RNA^Phe isoacceptors possess non‐identical set of identity elements at high and low Mg²⁺ concentration

FEBS Letters (1997)

Natalia Kholod Natalia V Pan'kova Sergey G. Mayorov A.I. Krutilina M. G. Shlyapnikov

Primary structures of phage T5- and Escherichia coli-encoded tRNA(Phe) are distinct at four out of 11 positions known as identity elements for E. coli phenylalanyl-tRNA synthetase (FRS). In order to reveal structural requirements for FRS recognition, aminoacylation of wild-type phage T5 tRNA(Phe) gene transcript and mutants containing substitutions of the identity elements at positions 20, 34, 35 and 36 was compared with E. coli tRNA(Phe) gene transcript. The wild-type phage T5 transcript can be aminoacylated with the same catalytic efficiency as the E. coli counterpart. However, the maximal aminoacylation rate for T5 and E. coli transcripts was reached at different Mg2+ concentrations: 4 and 15 mM, respectively. Aminoacylation assays with tRNA(Phe) mutants revealed that (i) phage transcripts with the substituted anticodon bases at positions 35 and 36 were efficient substrates for aminoacylation at 15 mM Mg2+ but not at optimal 4 mM Mg2+; (ii) any change of G34 in phage transcripts dramatically decreased the aminoacylation efficiency at both 4 and 15 mM Mg2+ whereas G34A mutation in the E. coli transcript exhibits virtually no influence on aminoacylation rate at 15 mM Mg2+; (iii) substitution of A20 with U in the phage transcript caused no significant change in the aminoacylation rate at both Mg2+ concentrations; (iv) phage transcripts with double substitutions A20U+A35C and A20U+A36C were very poor substrates for FRS. Collectively, the results indicate the non-identical mode of tRNA(Phe) recognition by E. coli FRS at low and high Mg2+ concentrations. Probably, along with identity elements, the local tRNA conformation is essential for recognition by FRS.

Aminoacylation

10.1016/s0014-5793(97)00608-x

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Citations (19)

Preparation of active tRNA gene transcripts devoid of 3'-extended products and dimers

Nucleic Acids Research (1998)

Natalia Kholod Konstantin Vassilenko M. G. Shlyapnikov В. Н. Ксензенко Lev L. Kisselev

Significant amounts (10–30%) of 3′-extended products with one or two extra nucleotides are synthesized in the course of run-off tRNA gene transcription with T7 RNA polymerase. Denaturing polyacrylamide gel electrophoresis appeared to be insufficient to provide preparative amounts of pure correct-size transcripts. Formation of dimers by tRNA gene transcripts as side products in the course of their activation is also another obstacle in preparation of biologically active transcripts. Here, we have shown that EF-Tu affinity chromatography and/or non-denaturing electrophoresis are simple and efficient tools for isolation of highly active correct-size transcripts. Conditions for transcript activation in vitro should be carefully controlled to prevent dimer formation and obtain reliable data on tRNA transcript structure and function.

Transcription

T7 RNA polymerase

10.1093/nar/26.10.2500

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Citations (20)

Dominant phylotypes in the 16S rRNA gene clone libraries from bacterial mats of the Uzon caldera (Kamchatka, Russia) hydrothermal springs

Microbiology (2013)

V. N. Akimov Olga A. Podosokorskaya M. G. Shlyapnikov В. Ф. Гальченко

Phylotype

Caldera

clone (Java method)

Library

10.1134/s0026261713060027

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Citations (9)