Saulius Klimasauskas

Summary

Affiliation: Institute of Biotechnology
Country: Lithuania

Publications

  1. ncbi request reprint Targeted labeling of DNA by methyltransferase-directed transfer of activated groups (mTAG)
    Grazvydas Lukinavicius
    Laboratory of Biological DNA Modification, Institute of Biotechnology, Graiciuno 8, LT 02241 Vilnius, Lithuania
    J Am Chem Soc 129:2758-9. 2007
  2. ncbi request reprint A new tool for biotechnology: AdoMet-dependent methyltransferases
    Saulius Klimasauskas
    Laboratory of Biological DNA Modification, Institute of Biotechnology, LT 02241 Vilnius, Lithuania
    Trends Biotechnol 25:99-104. 2007
  3. pmc Probing a rate-limiting step by mutational perturbation of AdoMet binding in the HhaI methyltransferase
    Egle Merkiene
    Laboratory of Biological DNA Modification, Institute of Biotechnology LT 02241 Vilnius, Lithuania
    Nucleic Acids Res 33:307-15. 2005
  4. ncbi request reprint HhaI DNA methyltransferase uses the protruding Gln237 for active flipping of its target cytosine
    Dalia Daujotyte
    Laboratory of Biological DNA Modification, Institute of Biotechnology, LT 02241 Vilnius, Lithuania
    Structure 12:1047-55. 2004
  5. doi request reprint Mechanistic insights into small RNA recognition and modification by the HEN1 methyltransferase
    Alexandra Plotnikova
    Department of Biological DNA Modification, Institute of Biotechnology, Vilnius University, Vilnius LT 02241, Lithuania
    Biochem J 453:281-90. 2013
  6. doi request reprint Cytosine-5-methyltransferases add aldehydes to DNA
    Zita Liutkeviciute
    Laboratory of Biological DNA Modification, Institute of Biotechnology, Vilnius, Lithuania
    Nat Chem Biol 5:400-2. 2009
  7. pmc Functional mapping of the plant small RNA methyltransferase: HEN1 physically interacts with HYL1 and DICER-LIKE 1 proteins
    Simona Baranauskė
    Department of Biological DNA Modification, Institute of Biotechnology, Vilnius University, Vilnius LT 02241, Lithuania
    Nucleic Acids Res 43:2802-12. 2015
  8. pmc A directed evolution design of a GCG-specific DNA hemimethylase
    Ruta Gerasimaite
    Laboratory of Biological DNA Modification, Institute of Biotechnology, Graiciuno 8, LT 02241 Vilnius, Lithuania
    Nucleic Acids Res 37:7332-41. 2009
  9. pmc Engineering the DNA cytosine-5 methyltransferase reaction for sequence-specific labeling of DNA
    Grazvydas Lukinavicius
    Department of Biological DNA Modification, Institute of Biotechnology, Vilnius University, 02241 Vilnius, Lithuania
    Nucleic Acids Res 40:11594-602. 2012
  10. pmc Direct observation of cytosine flipping and covalent catalysis in a DNA methyltransferase
    Ruta Gerasimaite
    Department of Biological DNA Modification, Institute of Biotechnology, Vilnius University, LT 02241 Vilnius, Lithuania
    Nucleic Acids Res 39:3771-80. 2011

Collaborators

  • Giedrius Vilkaitis
  • Edita Kriukiene
  • Ceslovas Venclovas
  • Thomas Szyperski
  • Ting Wang
  • Irina Artsimovitch
  • Arvydas Lubys
  • Béatrice Clouet-d'Orval
  • Saulius Grazulis
  • D T Dryden
  • Grazvydas Lukinavicius
  • Zita Liutkeviciute
  • Dalia Daujotyte
  • Alexandra Plotnikova
  • Ruta Gerasimaite
  • Viktoras Masevicius
  • Simona Baranauskė
  • Giedre Urbanaviciute
  • Migle Tomkuviene
  • Egle Merkiene
  • Elmar Weinhold
  • Rasa Rakauskaite
  • Christian Dalhoff
  • Nataliya Miropolskaya
  • Aleksandr Osipenko
  • Oksana M Subach
  • Robert K Neely
  • Audronė Rukšėnaitė
  • Andreas Finke
  • Robertas Juškėnas
  • Milda Mickutė
  • Milda Rudytė
  • Janina Ličytė
  • Andrey Kulbachinskiy
  • Vadim Nikiforov
  • Daria Esyunina
  • Ignas Cerniauskas
  • Audrone Lapinaite
  • Gintautas Tamulaitis
  • Nicholas E Geacintov
  • Alexander Kolbanovskiy
  • Vidmantas Lapiene
  • Zdislav Stasevskij
  • Elizaveta S Gromova
  • Diana V Maltseva
  • Anant Shastry
  • Steven W Magennis
  • Anita C Jones
  • Saulius Serva
  • Laura Manelyte
  • Jack Skalicky

Detail Information

Publications25

  1. ncbi request reprint Targeted labeling of DNA by methyltransferase-directed transfer of activated groups (mTAG)
    Grazvydas Lukinavicius
    Laboratory of Biological DNA Modification, Institute of Biotechnology, Graiciuno 8, LT 02241 Vilnius, Lithuania
    J Am Chem Soc 129:2758-9. 2007
  2. ncbi request reprint A new tool for biotechnology: AdoMet-dependent methyltransferases
    Saulius Klimasauskas
    Laboratory of Biological DNA Modification, Institute of Biotechnology, LT 02241 Vilnius, Lithuania
    Trends Biotechnol 25:99-104. 2007
    ..This paves the way for numerous novel applications in the functional analysis of biological methylation, biotechnology and medical diagnostics...
  3. pmc Probing a rate-limiting step by mutational perturbation of AdoMet binding in the HhaI methyltransferase
    Egle Merkiene
    Laboratory of Biological DNA Modification, Institute of Biotechnology LT 02241 Vilnius, Lithuania
    Nucleic Acids Res 33:307-15. 2005
    ..Our analysis indicates that the rate-limiting breakdown of a long-lived ternary product complex is initiated by the dissociation of AdoHcy or the opening of the catalytic loop in the enzyme...
  4. ncbi request reprint HhaI DNA methyltransferase uses the protruding Gln237 for active flipping of its target cytosine
    Dalia Daujotyte
    Laboratory of Biological DNA Modification, Institute of Biotechnology, LT 02241 Vilnius, Lithuania
    Structure 12:1047-55. 2004
    ..Gln237 thus plays a key role in actively opening the target C:G pair by a "push-and-bind" mechanism...
  5. doi request reprint Mechanistic insights into small RNA recognition and modification by the HEN1 methyltransferase
    Alexandra Plotnikova
    Department of Biological DNA Modification, Institute of Biotechnology, Vilnius University, Vilnius LT 02241, Lithuania
    Biochem J 453:281-90. 2013
    ..The results of the present study thus provide novel insights into the mechanism of RNA recognition and modification by a representative small RNA 2'-O-methyltransferase. ..
  6. doi request reprint Cytosine-5-methyltransferases add aldehydes to DNA
    Zita Liutkeviciute
    Laboratory of Biological DNA Modification, Institute of Biotechnology, Vilnius, Lithuania
    Nat Chem Biol 5:400-2. 2009
    ....
  7. pmc Functional mapping of the plant small RNA methyltransferase: HEN1 physically interacts with HYL1 and DICER-LIKE 1 proteins
    Simona Baranauskė
    Department of Biological DNA Modification, Institute of Biotechnology, Vilnius University, Vilnius LT 02241, Lithuania
    Nucleic Acids Res 43:2802-12. 2015
    ..On the basis of these findings, we propose a mechanism of plant miRNA maturation which involves binding of the HEN1 methyltransferase to the DCL1•HYL1•miRNA complex excluding the SERRATE protein. ..
  8. pmc A directed evolution design of a GCG-specific DNA hemimethylase
    Ruta Gerasimaite
    Laboratory of Biological DNA Modification, Institute of Biotechnology, Graiciuno 8, LT 02241 Vilnius, Lithuania
    Nucleic Acids Res 37:7332-41. 2009
    ..The designed C5-MTase can be used to produce hemimethylated CpG sites in DNA, which are valuable substrates for studies of mammalian maintenance MTases...
  9. pmc Engineering the DNA cytosine-5 methyltransferase reaction for sequence-specific labeling of DNA
    Grazvydas Lukinavicius
    Department of Biological DNA Modification, Institute of Biotechnology, Vilnius University, 02241 Vilnius, Lithuania
    Nucleic Acids Res 40:11594-602. 2012
    ....
  10. pmc Direct observation of cytosine flipping and covalent catalysis in a DNA methyltransferase
    Ruta Gerasimaite
    Department of Biological DNA Modification, Institute of Biotechnology, Vilnius University, LT 02241 Vilnius, Lithuania
    Nucleic Acids Res 39:3771-80. 2011
    ..These findings provide new insights into the temporal mechanism of this physiologically important reaction and pave the way to in-depth studies of other base-flipping systems...
  11. doi request reprint Selective covalent labeling of miRNA and siRNA duplexes using HEN1 methyltransferase
    Alexandra Plotnikova
    Institute of Biotechnology, Vilnius University, LT 02241 Vilnius, Lithuania
    J Am Chem Soc 136:13550-3. 2014
    ..The presented approach permits selective and efficient covalent labeling of small RNA duplexes with a variety of functional or reporter groups for their enrichment and analysis. ..
  12. doi request reprint DNA unmethylome profiling by covalent capture of CpG sites
    Edita Kriukiene
    Department of Biological DNA Modification, Institute of Biotechnology, Vilnius University, Vilnius LT 02241, Lithuania
    Nat Commun 4:2190. 2013
    ....
  13. pmc Programmable sequence-specific click-labeling of RNA using archaeal box C/D RNP methyltransferases
    Migle Tomkuviene
    Department of Biological DNA Modification, Institute of Biotechnology, Vilnius University, Vilnius LT 02241, Lithuania
    Nucleic Acids Res 40:6765-73. 2012
    ..The described approach for the first time permits synthetically tunable sequence-specific labeling of RNA with single-nucleotide precision...
  14. doi request reprint Biosynthetic selenoproteins with genetically-encoded photocaged selenocysteines
    Rasa Rakauskaite
    Institute of Biotechnology, Vilnius University, V Graiciuno 8, Vilnius LT 02241, Lithuania
    Chem Commun (Camb) 51:8245-8. 2015
    ....
  15. pmc Kinetic and functional analysis of the small RNA methyltransferase HEN1: the catalytic domain is essential for preferential modification of duplex RNA
    Giedrius Vilkaitis
    Laboratory of Biological DNA Modification, Institute of Biotechnology, Vilnius, Lithuania
    RNA 16:1935-42. 2010
    ....
  16. pmc Chemical mapping of cytosines enzymatically flipped out of the DNA helix
    Dalia Daujotyte
    Institute of Biotechnology, Graiciuno 8, LT 02241 Vilnius, Lithuania
    Nucleic Acids Res 36:e57. 2008
    ..Ecl18kI and R.PspGI, which represent a novel class of base-flipping enzymes. Our results thus offer a simple and convenient laboratory tool for detection and mapping of flipped-out cytosines in protein-DNA complexes...
  17. doi request reprint Direct decarboxylation of 5-carboxylcytosine by DNA C5-methyltransferases
    Zita Liutkeviciute
    Department of Biological DNA Modification, Institute of Biotechnology, Vilnius University, 02241 Vilnius, Lithuania
    J Am Chem Soc 136:5884-7. 2014
    ..The observed atypical enzymatic C-C bond cleavage reaction provides a plausible precedent for a direct reversal of caC to the unmodified state in DNA and offers a unique approach for sequence-specific analysis of genomic caC. ..
  18. pmc Circular permutation of DNA cytosine-N4 methyltransferases: in vivo coexistence in the BcnI system and in vitro probing by hybrid formation
    Giedrius Vilkaitis
    Institute of Biotechnology, GraiQióno 8, LT 2028 Vilnius, Lithuania
    Nucleic Acids Res 30:1547-57. 2002
    ..Our data illustrate that recombination of two related sequences by circular permutation may serve as an evolutionary mechanism for creating new specificities of amino MTases...
  19. doi request reprint Enhanced chemical stability of adomet analogues for improved methyltransferase-directed labeling of DNA
    Grazvydas Lukinavicius
    Institute of Biotechnology, Vilnius University, LT 02241 Vilnius, Lithuania
    ACS Chem Biol 8:1134-9. 2013
    ....
  20. pmc 5-Hydroxymethylcytosine--the elusive epigenetic mark in mammalian DNA
    Edita Kriukiene
    Department of Biological DNA Modification, Institute of Biotechnology, Vilnius University, Graiciuno 8, LT 02241 Vilnius, Lithuania
    Chem Soc Rev 41:6916-30. 2012
    ..It also discusses the most recent data on biochemical and chemical aspects of the formation and further conversion of this nucleobase in DNA and its possible biological roles in cell differentiation, embryogenesis and brain function...
  21. ncbi request reprint Solubility engineering of the HhaI methyltransferase
    Dalia Daujotyte
    Laboratory of Biological DNA Modification, Institute of Biotechnology, LT 2028 Vilnius, Lithuania
    Protein Eng 16:295-301. 2003
    ..35 mM), (ii) high-quality 2D-[(15)N,(1)H] TROSY NMR spectra, and (iii) (15)N spin relaxation times evidencing the presence of a monomeric well-folded protein in solution...
  22. pmc Interplay between the trigger loop and the F loop during RNA polymerase catalysis
    Nataliya Miropolskaya
    Institute of Molecular Genetics, Russian Academy of Sciences, Moscow 123182, Russia, Molecular Biology Department, Biological Faculty, Moscow State University, Moscow 119991 Russia, Department of Biological DNA Modification, Institute of Biotechnology, Vilnius University, Vilnius 02241, Lithuania and Department of Microbiology, The Ohio State University, Columbus, OH 43210, USA
    Nucleic Acids Res 42:544-52. 2014
    ..Thus, functional interplay between the FL and TL is essential for various catalytic activities of RNAP and plays an adaptive role in catalysis by thermophilic and mesophilic enzymes. ..
  23. ncbi request reprint The stereochemistry of benzo[a]pyrene-2'-deoxyguanosine adducts affects DNA methylation by SssI and HhaI DNA methyltransferases
    Oksana M Subach
    Chemistry Department, Moscow State University, Russia
    FEBS J 274:2121-34. 2007
    ..However, the intercalated base-displaced (+)-cis adduct does not interfere with the minor-groove DNA-catalytic loop contacts, allowing near-normal binding of the MTases and undiminished k(cat) values...
  24. ncbi request reprint Synthesis of S-adenosyl-L-methionine analogs and their use for sequence-specific transalkylation of DNA by methyltransferases
    Christian Dalhoff
    Institute of Organic Chemistry, RWTH Aachen University, Landoltweg 1, D 52056 Aachen, Germany
    Nat Protoc 1:1879-86. 2006
    ..Using these protocols, sequence-specific functionalized DNA can be obtained within one to two weeks...
  25. pmc Time-resolved fluorescence of 2-aminopurine as a probe of base flipping in M.HhaI-DNA complexes
    Robert K Neely
    School of Chemistry, The University of Edinburgh, West Mains Road, Edinburgh EH9 3JJ, UK
    Nucleic Acids Res 33:6953-60. 2005
    ..Analysis of the AP fluorescence decay function reveals conformational heterogeneity in the DNA-enzyme complexes that cannot be discerned from the present X-ray structures...