die('
Site is under construction
Dear site users
Site is under construction.
The site will be ready in less than 24 hours.
We are sorry for the inconvenience.
www.yektaweb.com
');
Reports of Biochemistry and Molecular Biology
rbmb.net
Basic Sciences
http://rbmb.net
1
admin
2322-3480
2322-3480
10.61882/rbmb
en
jalali
1398
10
1
gregorian
2020
1
1
8
4
online
1
fulltext
en
Swapping of The N-Terminal Domain of Human Topoisomerase 1B with the Corresponding Plasmodium Falciparum Counterpart Strongly Impairs Enzyme Activity
زیست شناسی ملکولی
Molecular Biology
مقالات اصلی
Original Article
<div style="text-align: justify;"><strong><em>Background:</em></strong> DNA topoisomerases 1B are a class of ubiquitous enzyme that solves the topological problems associated with biological processes such as replication, transcription and recombination. Numerous sequence alignment of topoisomerase 1B from different species shows that the lengths of different domains as well as their amino acids sequences are quite different. In the present study a hybrid enzyme, generated by swapping the N-terminal of <em>Plasmodium falciparum</em> into the corresponding domain of the human, has been characterized.<br>
<br>
<strong><em>Methods:</em></strong> The chimeric enzyme was generated using different sets of PCR. The <em>in vitro</em> characterization was carried out using different DNA substrate including radio-labelled oligonucleotides.<br>
<br>
<strong><em>Results:</em></strong> The chimeric enzyme displayed slower relaxation activity, cleavage and re-ligation kinetics strongly perturbed when compared to the human enzyme.<br>
<br>
<strong><em>Conclusions:</em></strong> These results indicate that the N-terminal domain has a crucial role in modulating topoisomerase activity in different species.<br>
</div>
N-terminal domain, Plasmodium falciparum topoisomerase 1B, Topoisomerase 1B.
366
375
http://rbmb.net/browse.php?a_code=A-10-286-3&slc_lang=en&sid=1
Jagadish Babu
Dasari
jagadishdrdasari@gmail.com
100319475328460017406
100319475328460017406
No
Department of Biology, University of Rome Tor Vergata, Via Della Ricerca Scientifica 1, 00133 Rome, Italy.
Bini Chhetri
Soren
binichhetri.14@gmail.com
100319475328460017407
100319475328460017407
No
Department of Biology, University of Rome Tor Vergata, Via Della Ricerca Scientifica 1, 00133 Rome, Italy.
Alessio
Ottaviani
ottaviani.alessio25@gmail.com
100319475328460017408
100319475328460017408
No
Department of Biology, University of Rome Tor Vergata, Via Della Ricerca Scientifica 1, 00133 Rome, Italy.
Cinzia
Tesauro
cinzia.tesauro@gmail.com
100319475328460017409
100319475328460017409
No
Department of Biology, University of Rome Tor Vergata, Via Della Ricerca Scientifica 1, 00133 Rome, Italy & Present address: Department of Molecular Biology and Genetics, University of Aarhus, C.F MøllersAllè 3, 8000 Aarhus C, Denmark.
Simona
Marino
simona_992@hotmail.it
100319475328460017410
100319475328460017410
No
Department of Biology, University of Rome Tor Vergata, Via Della Ricerca Scientifica 1, 00133 Rome, Italy.
Beatrice
Messina
beatrice.messina702@gmail.com
100319475328460017411
100319475328460017411
No
Department of Biology, University of Rome Tor Vergata, Via Della Ricerca Scientifica 1, 00133 Rome, Italy.
Paola
Fiorani
paola.fiorani@uniroma2.it
100319475328460017412
100319475328460017412
Yes
Department of Biology, University of Rome Tor Vergata, Via Della Ricerca Scientifica 1, 00133 Rome, Italy & Institute of Translational Pharmacology, National Research Council, CNR, Via Del Fosso del Cavaliere 100, Rome 00133, Italy.