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 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
  4. 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
  5. 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
  6. 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
  7. 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
  8. 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
  9. 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
  10. 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

Collaborators

Detail Information

Publications22

  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 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...
  4. 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...
  5. 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...
  6. 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
    ....
  7. 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...
  8. 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...
  9. 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...
  10. 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. ..
  11. 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
    ....
  12. 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...
  13. 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
    ....
  14. 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
    ....
  15. ncbi 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. ..
  16. 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
    ....
  17. 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...
  18. 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...
  19. 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. ..
  20. 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...
  21. 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...
  22. 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...