Počet záznamů: 1  

Conformational Diversity of Single-Stranded DNA from Bacterial Repetitive Extragenic Palindromes: Implications for the DNA Recognition Elements of Transposases

  1. 1.
    SYSNO ASEP0450981
    Druh ASEPJ - Článek v odborném periodiku
    Zařazení RIVJ - Článek v odborném periodiku
    Poddruh JČlánek ve WOS
    NázevConformational Diversity of Single-Stranded DNA from Bacterial Repetitive Extragenic Palindromes: Implications for the DNA Recognition Elements of Transposases
    Tvůrce(i) Charnavets, Tatsiana (BTO-N)
    Nunvář, Jaroslav (BTO-N)
    Nečasová, Iva (BTO-N)
    Voelker, J. (US)
    Breslauer, K.J. (US)
    Schneider, Bohdan (BTO-N) RID, ORCID
    Zdroj.dok.Biopolymers - ISSN 0006-3525
    Roč. 103, č. 10 (2015), s. 585-596
    Poč.str.10 s.
    Jazyk dok.eng - angličtina
    Země vyd.US - Spojené státy americké
    Klíč. slovabacterial repetitive extragenic palindromes (REP) ; circular dichroism spectroscopy ; REP associated tyrosine transposases (RAYTs)
    Vědní obor RIVEB - Genetika a molekulární biologie
    CEPED1.1.00/02.0109 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy
    GAP305/12/1801 GA ČR - Grantová agentura ČR
    EE2.3.30.0020 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy
    Institucionální podporaBTO-N - RVO:86652036
    UT WOS000358620900005
    DOI10.1002/bip.22666
    AnotaceRepetitive extragenic palindrome (REP)associated tyrosine transposase enzymes (RAYTs) bind REP DNA domains and catalyze their cleavage. Genomic sequence analyses identify potential noncoding REP sequences associated with RAYT-encoding genes. To probe the conformational space of potential RAYT DNA binding domains, we report here spectroscopic and calorimetric measurements that detect and partially characterize the solution conformational heterogeneity of REP oligonucleotides from six bacterial species. Our data reveal most of these REP oligonucleotides adopt multiple conformations, suggesting that RAYTs confront a landscape of potential DNA substrates in dynamic equilibrium that could be selected, enriched, and/or induced via differential binding. Thus, the transposase-bound DNA motif may not be the predominant conformation of the isolated REP domain. Intriguingly, for several REPs, the circular dichroism spectra suggest guanine tetraplexes as potential alternative or additional RAYT recognition elements, an observation consistent with these REP domains being highly nonrandom, with tetraplex-favoring 5-G and 3-C-rich segments. In fact, the conformational heterogeneity of REP domains detected and reported here, including the formation of noncanonical DNA secondary structures, may reflect a general feature required for recognition by RAYT transposases. Based on our biophysical data, we propose guanine tetraplexes as an additional DNA recognition element for binding by RAYT transposase enzymes
    PracovištěBiotechnologický ústav
    KontaktMonika Kopřivová, Monika.Koprivova@ibt.cas.cz, Tel.: 325 873 700
    Rok sběru2016
Počet záznamů: 1  

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