Projects funded by the NCN


Information on the principal investigator and host institution

Information of the project and the call

Keywords

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New 5-hydroxymethylcytosine binding proteins

2014/13/B/NZ1/03991

Keywords:

5-hydroxymethylcytosine mass-spectrometry protein-nucleic acid interactions leukemias

Descriptors:

  • NZ1_1: Molecular biology
  • NZ1_2: Biochemistry
  • NZ1_4: Structural biology

Panel:

NZ1 - Molecular biology, structural biology, biotechnology: molecular biology, structural biology, biotechnology

Host institution :

Międzynarodowy Instytut Biologii Molekularnej i Komórkowej

woj. mazowieckie

Other projects carried out by the institution 

Principal investigator (from the host institution):

prof. Matthias Bochtler 

Number of co-investigators in the project: 8

Call: OPUS 7 - announced on 2014-03-17

Amount awarded: 1 283 750 PLN

Project start date (Y-m-d): 2015-01-23

Project end date (Y-m-d): 2019-01-22

Project duration:: 48 months (the same as in the proposal)

Project status: Project settled

Information in the final report

  • Publication in academic press/journals (8)
  1. Activity and structure of EcoKMcrA.
    Authors:
    Czapinska H, Kowalska M, Zagorskaite E, Manakova E, Slyvka A, Xu SY, Siksnys V, Sasnauskas G, Bochtler M.
    Academic press:
    Nucleic Acids Research (rok: 2018, tom: 46(18), strony: 9829-9841), Wydawca: Oxford University Press
    Status:
    Published
    DOI:
    10.1093/nar/gky731 - link to the publication
  2. Nei-like 1 (NEIL1) excises 5-carboxylcytosine directly and stimulates TDG-mediated 5-formyl and 5-carboxylcytosine excision
    Authors:
    Anton Slyvka, Karolina Mierzejewska & Matthias Bochtler
    Academic press:
    Scientific Reports (rok: 2017, tom: 7, strony: 45304), Wydawca: NATURE PUBLISHING GROUP
    Status:
    Published
    DOI:
    10.1038/s41598-017-07458-4 - link to the publication
  3. The Bacteroidetes Q-Rule: Pyroglutamate in Signal Peptidase I Substrates.
    Authors:
    Bochtler M, Mizgalska D, Veillard F, Nowak ML, Houston J, Veith P, Reynolds EC, Potempa J.
    Academic press:
    Frontiers in Microbiology (rok: 2018, tom: 0,534722222222222, strony: 45304), Wydawca: Washington State University
    Status:
    Published
    DOI:
    10.3389/fmicb.2018.00230 - link to the publication
  4. The Y. bercovieri Anbu crystal structure sheds light on the evolution of highly (pseudo)symmetric multimers
    Authors:
    Anna Piasecka, Honorata Czapinska, Marie-Theres Vielberg, Roman H. Szczepanowski, Reiner Kiefersauer, Simon Reed, Michael Groll and Matthias Bochtler
    Academic press:
    Journal of Molecular Biology (rok: 2018, tom: 430, strony: 611-627), Wydawca: Elsevier
    Status:
    Published
    DOI:
    10.1016/j.jmb.2017.11.016 - link to the publication
  5. Unique mechanism of target recognition by PfoI restriction endonuclease of the CCGG-family.
    Authors:
    Tamulaitiene G, Manakova E, Jovaisaite V, Tamulaitis G, Grazulis S, Bochtler M, Siksnys V.
    Academic press:
    Nucleic Acids Research (rok: 2019, tom: 47(2), strony: 997-1010), Wydawca: Oxford University Press
    Status:
    Published
    DOI:
    10.1093/nar/gky1137 - link to the publication
  6. Crystal structure of the modification-dependent SRA-HNH endonuclease TagI.
    Authors:
    Kisiala M, Copelas A, Czapinska H, Xu SY, Bochtler M.
    Academic press:
    Nucleic Acids Research (rok: 2018, tom: 46(19), strony: 10489-10503), Wydawca: Oxford University Press
    Status:
    Published
    DOI:
    10.1093/nar/gky781 - link to the publication
  7. DNA demethylation pathways: Additional players and regulators.
    Authors:
    Bochtler M, Kolano A, Xu G-L
    Academic press:
    Bioessays (rok: 2017, tom: 39(1), strony: 45304), Wydawca: WILEY-BLACKWELL
    Status:
    Published
    DOI:
    10.1002/bies.201600178 - link to the publication
  8. On the role of steric clashes in methylation control of restriction endonuclease activity
    Authors:
    Mierzejewska K, Bochtler M, Czapinska H
    Academic press:
    Nucleic Acids Research (rok: 2016, tom: 44(1), strony: 485–495), Wydawca: Oxford University Press
    Status:
    Published
    DOI:
    10.1093/nar/gkv1341 - link to the publication