Molecular interactions between poly(ADP-ribose) polymerase (PARP I) and topoisomerase I (Topo I): Identification of topology of binding

Pal I. Bauer; Hui Je Chen; Erzsebet Kenesi; Istvan Kenessey; Kalman G. Buki; Eva Kirsten; Alaeddin Hakam; Jaulang I. Hwang; Ernest Kun

doi:10.1016/S0014-5793(01)02919-2

Molecular interactions between poly(ADP-ribose) polymerase (PARP I) and topoisomerase I (Topo I): Identification of topology of binding

Pal I. Bauer, Hui Je Chen, Erzsebet Kenesi, Istvan Kenessey, Kalman G. Buki, Eva Kirsten, Alaeddin Hakam, Jaulang I. Hwang, Ernest Kun

Research output: Contribution to journal › Article › peer-review

43 Citations (Scopus)

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	https://doi.org/10.1016/S0014-5793(01)02919-2
Publication status	Published - Oct 12 2001
Externally published	Yes

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

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(01)02919-2

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@article{f2147fd1d9884ef7bf140ca64d72995a,

title = "Molecular interactions between poly(ADP-ribose) polymerase (PARP I) and topoisomerase I (Topo I): Identification of topology of binding",

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.",

keywords = "Binding site, Poly(ADP-ribose) polymerase I, Topoisomerase I binding, Topoisomerase I regulation by poly(ADP-ribose) polymerase I, Topology interaction",

author = "Bauer, {Pal I.} and Chen, {Hui Je} and Erzsebet Kenesi and Istvan Kenessey and Buki, {Kalman G.} and Eva Kirsten and Alaeddin Hakam and Hwang, {Jaulang I.} and Ernest Kun",

note = "Funding Information: This work was supported by grants (to P.I.B.) TO 23959 and 29620 from OTKA (Hungarian Science Foundation) and by UC A2511 (from Syn-X Inc. Canada) obtained through Dr. George Jackowski (to E.K.). The stimulating discussions with Professor Charles Ordahl (Department of Anatomy, UCSF) are acknowledged with appreciation. The entire research project was originated while P.I.B., K.G.B., A.H., E.K. and E.K. were working in the Romberg Tiburon Centers of San Francisco State University (Tiburon, CA, USA) and completed by collaboration of the laboratories shown on the title page.",

year = "2001",

month = oct,

day = "12",

doi = "10.1016/S0014-5793(01)02919-2",

language = "English",

volume = "506",

pages = "239--242",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc.",

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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

N1 - Funding Information: This work was supported by grants (to P.I.B.) TO 23959 and 29620 from OTKA (Hungarian Science Foundation) and by UC A2511 (from Syn-X Inc. Canada) obtained through Dr. George Jackowski (to E.K.). The stimulating discussions with Professor Charles Ordahl (Department of Anatomy, UCSF) are acknowledged with appreciation. The entire research project was originated while P.I.B., K.G.B., A.H., E.K. and E.K. were working in the Romberg Tiburon Centers of San Francisco State University (Tiburon, CA, USA) and completed by collaboration of the laboratories shown on the title page.

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

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U2 - 10.1016/S0014-5793(01)02919-2

DO - 10.1016/S0014-5793(01)02919-2

M3 - Article

C2 - 11602253

AN - SCOPUS:0035850913

SN - 0014-5793

VL - 506

SP - 239

EP - 242

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

Molecular interactions between poly(ADP-ribose) polymerase (PARP I) and topoisomerase I (Topo I): Identification of topology of binding

Abstract

Keywords

ASJC Scopus subject areas

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