Abstract
The molecular interactions of poly(ADP-ribose) polymerase I (PARP I) and topoisomerase I (Topo I) have been determined by the analysis of physical binding of the two proteins and some of their polypeptide components and by the effect of PARP I on the enzymatic catalysis of Topo I. Direct association of Topo I and PARP I as well as the binding of two Topo I polypeptides to PARP I are demonstrated. The effect of PARP I on the 'global' Topo I reaction (scission and religation), and the activation of Topo I by the 36 kDa polypeptide of PARP I and catalytic modifications by poly(ADP-ribosyl)ation are also shown. The covalent binding of Topo I to circular DNA is activated by PARP I similar to the degree of activation of the 'global' Topo I reaction, whereas the religation of DNA is unaffected by PARP I. The geometry of PARP I-Topo I interaction compared to automodified PARP I was reconstructed from direct binding assays between glutathione S-transferase fusion polypeptides of Topo I and PARP I demonstrating highly selective binding, which was correlated with amino acid sequences and with the 'C clamp' model derived from X-ray crystallography.
| Original language | English |
|---|---|
| Pages (from-to) | 239-242 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 506 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Oct 12 2001 |
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Keywords
- Binding site
- Poly(ADP-ribose) polymerase I
- Topoisomerase I binding
- Topoisomerase I regulation by poly(ADP-ribose) polymerase I
- Topology interaction
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Molecular interactions between poly(ADP-ribose) polymerase (PARP I) and topoisomerase I (Topo I) : Identification of topology of binding. / Bauer, Pal I.; Chen, Hui Je; Kenesi, Erzsebet; Kenessey, Istvan; Buki, Kalman G.; Kirsten, Eva; Hakam, Alaeddin; Hwang, Jaulang I.; Kun, Ernest.
In: FEBS Letters, Vol. 506, No. 3, 12.10.2001, p. 239-242.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Molecular interactions between poly(ADP-ribose) polymerase (PARP I) and topoisomerase I (Topo I)
T2 - Identification of topology of binding
AU - Bauer, Pal I.
AU - Chen, Hui Je
AU - Kenesi, Erzsebet
AU - Kenessey, Istvan
AU - Buki, Kalman G.
AU - Kirsten, Eva
AU - Hakam, Alaeddin
AU - Hwang, Jaulang I.
AU - Kun, Ernest
PY - 2001/10/12
Y1 - 2001/10/12
N2 - The molecular interactions of poly(ADP-ribose) polymerase I (PARP I) and topoisomerase I (Topo I) have been determined by the analysis of physical binding of the two proteins and some of their polypeptide components and by the effect of PARP I on the enzymatic catalysis of Topo I. Direct association of Topo I and PARP I as well as the binding of two Topo I polypeptides to PARP I are demonstrated. The effect of PARP I on the 'global' Topo I reaction (scission and religation), and the activation of Topo I by the 36 kDa polypeptide of PARP I and catalytic modifications by poly(ADP-ribosyl)ation are also shown. The covalent binding of Topo I to circular DNA is activated by PARP I similar to the degree of activation of the 'global' Topo I reaction, whereas the religation of DNA is unaffected by PARP I. The geometry of PARP I-Topo I interaction compared to automodified PARP I was reconstructed from direct binding assays between glutathione S-transferase fusion polypeptides of Topo I and PARP I demonstrating highly selective binding, which was correlated with amino acid sequences and with the 'C clamp' model derived from X-ray crystallography.
AB - The molecular interactions of poly(ADP-ribose) polymerase I (PARP I) and topoisomerase I (Topo I) have been determined by the analysis of physical binding of the two proteins and some of their polypeptide components and by the effect of PARP I on the enzymatic catalysis of Topo I. Direct association of Topo I and PARP I as well as the binding of two Topo I polypeptides to PARP I are demonstrated. The effect of PARP I on the 'global' Topo I reaction (scission and religation), and the activation of Topo I by the 36 kDa polypeptide of PARP I and catalytic modifications by poly(ADP-ribosyl)ation are also shown. The covalent binding of Topo I to circular DNA is activated by PARP I similar to the degree of activation of the 'global' Topo I reaction, whereas the religation of DNA is unaffected by PARP I. The geometry of PARP I-Topo I interaction compared to automodified PARP I was reconstructed from direct binding assays between glutathione S-transferase fusion polypeptides of Topo I and PARP I demonstrating highly selective binding, which was correlated with amino acid sequences and with the 'C clamp' model derived from X-ray crystallography.
KW - Binding site
KW - Poly(ADP-ribose) polymerase I
KW - Topoisomerase I binding
KW - Topoisomerase I regulation by poly(ADP-ribose) polymerase I
KW - Topology interaction
UR - http://www.scopus.com/inward/record.url?scp=0035850913&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035850913&partnerID=8YFLogxK
U2 - 10.1016/S0014-5793(01)02919-2
DO - 10.1016/S0014-5793(01)02919-2
M3 - Article
C2 - 11602253
AN - SCOPUS:0035850913
VL - 506
SP - 239
EP - 242
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 3
ER -