Research output: Contribution to journal › Article › peer-review
Regulation of poly(ADP-Ribose) polymerase 1 activity by Y-Box-binding protein 1. / Naumenko, Konstantin N.; Sukhanova, Mariya V.; Hamon, Loic et al.
In: Biomolecules, Vol. 10, No. 9, 1325, 16.09.2020, p. 1-26.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - Regulation of poly(ADP-Ribose) polymerase 1 activity by Y-Box-binding protein 1
AU - Naumenko, Konstantin N.
AU - Sukhanova, Mariya V.
AU - Hamon, Loic
AU - Kurgina, Tatyana A.
AU - Alemasova, Elizaveta E.
AU - Kutuzov, Mikhail M.
AU - Pastré, David
AU - Lavrik, Olga I.
N1 - Publisher Copyright: © 2020 by the authors. Licensee MDPI, Basel, Switzerland.
PY - 2020/9/16
Y1 - 2020/9/16
N2 - Y-box-binding protein 1 (YB-1) is a multifunctional positively charged protein that interacts with DNA or RNA and poly(ADP-ribose) (PAR). YB-1 is poly(ADP-ribosyl)ated and stimulates poly(ADP-ribose) polymerase 1 (PARP1) activity. Here, we studied the mechanism of YB-1-dependent PAR synthesis by PARP1 in vitro using biochemical and atomic force microscopy assays. PAR synthesis activity of PARP1 is known to be facilitated by co-factors such as Mg2+. However, in contrast to an Mg2+-dependent reaction, the activation of PARP1 by YB-1 is accompanied by overall up-regulation of protein PARylation and shortening of the PAR polymer. Therefore, YB-1 and cation co-factors stimulated PAR synthesis in divergent ways. PARP1 autoPARylation in the presence of YB-1 as well as trans-PARylation of YB-1 are greatly affected by the type of damaged DNA, suggesting that PARP1 activation depends on the formation of a PARP1–YB-1–DNA ternary complex. An unstructured C-terminal part of YB-1 involved in an interaction with PAR behaves similarly to full-length YB-1, indicating that both DNA and PAR binding are involved in the stimulation of PARP1 activity by YB-1. Thus, YB-1 is likely linked to the regulation of PARylation events in cells via an interaction with PAR and damaged DNA.
AB - Y-box-binding protein 1 (YB-1) is a multifunctional positively charged protein that interacts with DNA or RNA and poly(ADP-ribose) (PAR). YB-1 is poly(ADP-ribosyl)ated and stimulates poly(ADP-ribose) polymerase 1 (PARP1) activity. Here, we studied the mechanism of YB-1-dependent PAR synthesis by PARP1 in vitro using biochemical and atomic force microscopy assays. PAR synthesis activity of PARP1 is known to be facilitated by co-factors such as Mg2+. However, in contrast to an Mg2+-dependent reaction, the activation of PARP1 by YB-1 is accompanied by overall up-regulation of protein PARylation and shortening of the PAR polymer. Therefore, YB-1 and cation co-factors stimulated PAR synthesis in divergent ways. PARP1 autoPARylation in the presence of YB-1 as well as trans-PARylation of YB-1 are greatly affected by the type of damaged DNA, suggesting that PARP1 activation depends on the formation of a PARP1–YB-1–DNA ternary complex. An unstructured C-terminal part of YB-1 involved in an interaction with PAR behaves similarly to full-length YB-1, indicating that both DNA and PAR binding are involved in the stimulation of PARP1 activity by YB-1. Thus, YB-1 is likely linked to the regulation of PARylation events in cells via an interaction with PAR and damaged DNA.
KW - Poly(ADP-ribose) polymerase 1
KW - Protein poly(ADP-ribosyl)ation
KW - Y-box-binding protein 1
UR - http://www.scopus.com/inward/record.url?scp=85090893255&partnerID=8YFLogxK
U2 - 10.3390/biom10091325
DO - 10.3390/biom10091325
M3 - Article
C2 - 32947956
AN - SCOPUS:85090893255
VL - 10
SP - 1
EP - 26
JO - Biomolecules
JF - Biomolecules
SN - 2218-273X
IS - 9
M1 - 1325
ER -
ID: 25290512