M. A. Tukalo

ORCID: 0000-0002-0982-2372
Publications
Citations
Views
---
Saved
---
About
Contact & Profiles
Research Areas
  • RNA and protein synthesis mechanisms
  • RNA modifications and cancer
  • Enzyme Structure and Function
  • Genomics and Phylogenetic Studies
  • Bacterial Genetics and Biotechnology
  • Tuberculosis Research and Epidemiology
  • RNA Research and Splicing
  • Chemical Synthesis and Analysis
  • Cancer-related molecular mechanisms research
  • Protein Structure and Dynamics
  • RNA regulation and disease
  • Amino Acid Enzymes and Metabolism
  • Mass Spectrometry Techniques and Applications
  • Antimicrobial Peptides and Activities
  • ATP Synthase and ATPases Research
  • Machine Learning in Bioinformatics
  • Biochemical and Molecular Research
  • Cancer Genomics and Diagnostics
  • Mycobacterium research and diagnosis
  • Genetic factors in colorectal cancer
  • Microbial Metabolic Engineering and Bioproduction
  • DNA and Nucleic Acid Chemistry
  • Colorectal Cancer Treatments and Studies
  • Nutrition, Genetics, and Disease
  • Biopolymer Synthesis and Applications

Institute of Molecular Biology and Genetics
2016-2025

Institute of Software Systems
2019-2025

National Academy of Sciences of Ukraine
2000-2023

DeVry University
2023

Instituto de Biomedicina y Genética Molecular de Valladolid
2019

European Molecular Biology Laboratory
1997-2012

University of Illinois Urbana-Champaign
2009

Shanghai Jiao Tong University
2007

Stanford University
2007

Institut Laue-Langevin
2005

Aminoacyl-transfer RNA (tRNA) synthetases, which catalyze the attachment of correct amino acid to its corresponding tRNA during translation genetic code, are proven antimicrobial drug targets. We show that broad-spectrum antifungal 5-fluoro-1,3-dihydro-1-hydroxy-2,1-benzoxaborole (AN2690), in development for treatment onychomycosis, inhibits yeast cytoplasmic leucyl-tRNA synthetase by formation a stable tRNA(Leu)-AN2690 adduct editing site enzyme. Adduct is mediated through boron atom AN2690...

10.1126/science.1142189 article EN Science 2007-06-21

The crystal structure of Thermus thermophilus seryl-transfer RNA synthetase, a class 2 aminoacyl-tRNA complexed with single tRNA(Ser) molecule was solved at 2.9 A resolution. revealed how insertion conserved base G20b from the D loop into core tRNA determines orientation long variable arm, which is characteristic feature most serine specific tRNAs. On binding, antiparallel coiled-coil domain one subunit synthetase makes contacts arm and T psi C directs acceptor stem active site other...

10.1126/science.8128220 article EN Science 1994-03-11

Crystal structures of seryl-tRNA synthetase from Thermus thermophilus complexed with two different analogs seryl adenylate have been determined at 2.5 A resolution. The first complex is between the enzyme and seryl-hydroxamate-AMP (adenosine monophosphate), produced enzymatically in crystal adenosine triphosphate (ATP) serine hydroxamate, second a synthetic analog (5'-O-[N-(L-seryl)-sulfamoyl]adenosine), which strong inhibitor enzyme. Both molecules are bound similar fashion by network...

10.1126/science.8128224 article EN Science 1994-03-11

The crystal structure at 2.7 Å resolution of histidyl-tRNA synthetase (HisRS) from Thermus thermophilus in complex with its amino acid substrate histidine has been determined. In the asymmetric unit there are two homodimers, each subunit containing 421 residues. Each monomer enzyme consists three domains: (1) an N-terminal catalytic domain a six-stranded antiparallel β-sheet and motifs common to all class II aminoacyl-tRNA synthetases, (2) 90-residue C-terminal α/β which is most IIa...

10.1021/bi9618373 article EN Biochemistry 1997-03-01

Eukaryotic elongation factor eEF1A transits between the GTP- and GDP-bound conformations during ribosomal polypeptide chain elongation. eEF1A*GTP establishes a complex with aminoacyl-tRNA in A site of 80S ribosome. Correct codon–anticodon recognition triggers GTP hydrolysis, subsequent dissociation eEF1A*GDP from The structures both 'GTP'- 'GDP'-bound are unknown. Thus, eEF1A-related mechanisms were anticipated only by analogy bacterial homolog EF-Tu. Here, we report first crystal structure...

10.1093/nar/gku974 article EN cc-by-nc Nucleic Acids Research 2014-10-17

Using in vitro tRNA transcripts and minihelices it was shown that the tyrosine identity for charging by tyrosyl-tRNA synthetase (TyrRS) from archaeon Methanococcus jannaschii is determined six nucleotides: discriminator base A73 first base-pair C1-G72 acceptor stem together with anticodon triplet. The residues however, participate only weakly determination, especially 35 36. completeness of aforementioned set verified its tranfer into several tRNAs which then become as efficiently...

10.1046/j.1432-1327.2001.01931.x article EN European Journal of Biochemistry 2001-02-01

A screen of 37 compounds identified four inhibitors that exhibited dual on-target activity against <italic>Mycobacterium tuberculosis</italic> aminoacyl-tRNA synthetases.

10.1039/c9md00347a article EN MedChemComm 2019-01-01

Tuberculosis has become the world's most lethal infectious disease. A major challenge in treating tuberculosis is multidrug resistance of Mycobacterium to existing antibiotics. Therefore, there an urgent need discover new antituberculosis agents with unexploited mechanisms action. The aim work was develop inhibitors mycobacterial leucyl-tRNA synthetase (LeuRS) antibacterial activity. virtual screening compound collection containing about 250,000 ligands into aminoacyl-adenylate binding site...

10.1080/17568919.2025.2485673 article EN Future Medicinal Chemistry 2025-04-21

The increase of antibiotic resistance amongst Mycobacterium tuberculosis strains has become one the most pressing problems modern medicine. Therefore, search antibiotics against M. with novel mechanisms action is very important. We have identified inhibitors leucyl-tRNA synthetase (LeuRS) among derivatives 5-phenylamino-2H-[1,2,4]triazin-3-one. active compounds 5-(5-chloro-2-hydroxy-phenylamino)-6-methyl-2H-[1,2,4]triazin-3-one and 5-(5-chloro-2-hydroxy-phenylamino)-2H-[1,2,4]triazin-3-one...

10.1080/14756366.2016.1190712 article EN Journal of Enzyme Inhibition and Medicinal Chemistry 2016-05-31

A new approach allowing detection of contact points between RNAs and proteins has been developed using trans-diamminedichloroplatinum(II) as the cross-linking reagent. The advantage method relies on fact that coordination bonds platinum potential acceptors nucleic acids (mainly S cysteine or methionine residues; N imidazole rings in histidine N7 guanine, N1 adenine, N3 cytosine residues) can be reversed, so cross-linked oligonucleotides peptides within a complex analyzed directly. was worked...

10.1021/bi00390a045 article EN Biochemistry 1987-08-01

Translation elongation factor eEF1A2 was purified to homogeneity from rabbit muscle by two consecutive ion-exchange column-chromatography steps and this mammalian successfully crystallized for the first time. Protein crystals obtained using ammonium sulfate as precipitant diffracted 2.5 Å resolution belonged space group P6(1)22 or P6(3)22 (unit-cell parameters a = b 135.4, c 304.6 Å). A complete native data set collected 2.7 resolution.

10.1107/s1744309112000243 article EN Acta Crystallographica Section F Structural Biology and Crystallization Communications 2012-02-21
Coming Soon ...