Paper
RSC Advances
centrin and DNA, which can result in abolishment of stimula-
tion.68 Based on the reported literature, the binding and
cleavage activity of centrin to DNA represented currently may
link to the functions within nucleus or NER. The activity may be
enhanced in the presence of XPC. The research provides clues
for further work. However, much more work remain needs to be
done because it is unclear for the precise roles of centrin played
in the process.
5 B. Y. Jiang, M. Wang, F. Z. Li, L. Yu and J. Q. Xie, Biosens.
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6 A. D. Robison and I. J. Finkelstein, FEBS Lett., 2014, 588,
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7 N. M. Luscombe, R. A. Laskowski and J. M. Thornton, Nucleic
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4 Conclusion
10 R. Molina, P. Redondo, S. Stella, M. Marenchino,
M. D'Abramo, F. L. Gervasio, J. C. Epinat, J. Valton,
S. Grizot, P. Duchateau, J. Prieto and G. Montoya, Nucleic
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In summary, N-EoCen has been found to exhibit unusual
affinity to double stranded DNA. The binding constants of
holoN-EoCen and DNA are higher than that of apoN-EoCen
under the same condition. The interaction prole probably 11 Z. Q. Deng, Q. Wang, Z. Liu, M. F. Zhang, A. C. D. Machado,
may be that one protein molecular bind with one DNA molec-
ular involved in about 35 bp. The binding of protein to the helix
is entirely controlled by entropy change. Ultimately, the helix
T. P. Chiu, C. Feng, Q. Zhang, L. Yu, L. Qi, J. G. Zheng,
X. Wang, X. M. Huo, X. X. Qi, X. R. Li, W. Wu, R. Rohs,
Y. Li and Z. Z. Chen, Nat. Commun., 2015, 6, 7462.
structure of DNA is subjected to perturbation. Meanwhile, the 12 L. Jen-Jacobson, Biopolymers, 1997, 44, 153–180.
protein secondary structure as well as the Tyr environment 13 S. S. Narayanan and S. K. Pal, Langmuir, 2007, 23, 6712–6718.
changes to a large extent. More interestingly, N-EoCen exhibits 14 R. Errabolu, M. A. Sanders and J. L. Salisbury, J. Cell Sci.,
endonuclease-like activity to DNA via a hydrolysis pathway. Ser
and Thr, in particular Ser22, may be primarily responsible for 15 T. Fischer, S. Rodriguez-Navarro, G. Pereira, A. Racz,
DNA cleavage under these conditions. The exibility of Ser E. Schiebel and E. Hurt, Nat. Cell Biol., 2004, 6, 840–848.
located at 22 of EF-hand domains may explain the differences in 16 K. K. Resendes, B. A. Rasala and A. D. J. Forbes, Mol. Cell.
cleavage activity between apoN-EoCen and holoN-EoCen. Note
Biol., 2008, 28, 1755–1769.
that the cleavage products are mainly nicked circular DNA for 17 L. Radu, I. Durussel, L. Assairi, Y. Blouquit, S. Miron,
1994, 107, 9–16.
holoN-EoCen and linear DNA for apoN-EoCen, respectively. To
date, there has been no evidence for the biochemical role of N-
J. A. Cox and C. T. Craescu, Biochemistry, 2010, 49, 4383–
4394.
EoCen–DNA reaction. It is possible to relate to the cellular 18 T. J. Dantas, O. M. Daly, P. C. Conroy, M. Tomas, Y. Wang,
function of the protein in NER. The results on the protein–DNA
interaction may nd its future importance in the investigation
of centrin more features.
P. Lalor, P. Dockery, E. Ferrando-May and C. G. Morrison,
PLoS One, 2013, 8, e68487.
19 T. J. Dantas, O. M. Daly and C. G. Morrison, Cell. Mol. Life
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20 A. Paoletti, M. Moudjou, M. Paintrand, J. L. Salisbury and
M. Bornens, J. Cell Sci., 1996, 109, 3089–3102.
21 L. Liang, S. Flury, V. Kalck, B. Hohn and J. Molinier, Plant
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Conflicts of interest
There are no conicts to declare.
22 T. J. Dantas, Y. Wang, P. Lalor, P. Dockery and
C. G. Morrison, J. Cell Biol., 2011, 193, 307–318.
Acknowledgements
This work was supported by the National Natural Science 23 M. Araki, C. Masutani, M. Takemura, A. Uchida,
Foundation of PR China [grant numbers 20771068, No.
20901048 and No. 21571117], the PhD Programs Foundation of
K. Sugasawa, J. Kondoh, Y. Ohkuma and F. Hanaoka, J.
Biol. Chem., 2001, 276, 18665–18672.
the Ministry of Education of China (grant number 24 R. Nishi, W. Sakai, D. Tone, F. Hanaoka and K. Sugasawa,
20131401110011). We thank T. Zhang of scientic instrument Nucleic Acids Res., 2013, 41, 6917–6929.
center of Shanxi University for her excellent technical assistance 25 E. X. Shi, W. L. Zhang, Y. Q. Zhao and B. S. Yang, RSC Adv.,
in ITC.
2017, 7, 27139–27149.
´
26 M. R. Beccia, S. S. Merle, D. Lemaire, N. Bremond,
R. Pardoux, S. Blangy, P. Guilbaud and C. Berthomieu, J.
Biol. Inorg Chem., 2015, 20, 905–919.
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