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1.
FIG. 2

FIG. 2. From: XRCC1 Is Specifically Associated with Poly(ADP-Ribose) Polymerase and Negatively Regulates Its Activity following DNA Damage.

XRCC1 NLS. Cos-7 cells were transfected with the empty vector pCHK (a) or with the construct pCHK-NLS-XRCC1-(239–266), which encodes the XRCC1 bipartite NLS fused to β-galactosidase (b). The subcellular localization of the recombinant proteins was assessed by histochemical staining with X-Gal (5-bromo-4-chloro-3-indolyl-β-d-galactopyranoside). Micrographs of Cos-7 cells transfected with the XRCC1 putative NLS exclusively displayed blue nuclei (b).

Murielle Masson, et al. Mol Cell Biol. 1998 June;18(6):3563-3571.
2.
FIG. 6

FIG. 6. From: XRCC1 Is Specifically Associated with Poly(ADP-Ribose) Polymerase and Negatively Regulates Its Activity following DNA Damage.

ADP-ribosylation of XRCC1 and its effect on PARP auto-poly(ADP-ribosylation). Incubations of XRCC1 with 300 ng of purified PARP were performed with 1 μM [32P]NAD for 2 min at 25°C under standard conditions (38). Acid-insoluble products were separated by gel electrophoresis and revealed by autoradiography of the stained and dried gel. Lane 1, PARP alone; lanes 2 to 5, purified His-tagged XRCC1 added at the indicated molar ratios with respect to PARP. (ADPR)n, ADP-ribosylation.

Murielle Masson, et al. Mol Cell Biol. 1998 June;18(6):3563-3571.
3.
FIG. 5

FIG. 5. From: XRCC1 Is Specifically Associated with Poly(ADP-Ribose) Polymerase and Negatively Regulates Its Activity following DNA Damage.

In vitro negative regulation of PARP activity by XRCC1. (A) PARP activities were determined in total extracts of Cos-7 cells expressing either GST or GST–XRCC1-(170–428), as described in Materials and Methods. (B) Immunoblot detection of GST (lanes 1 and 2) and PARP (lanes 3 and 4) in extracts from Cos-7 cells transfected either with pBC-NLS (lanes 1 and 3) or with pBC XRCC1-(170–428) (lanes 2 and 4).

Murielle Masson, et al. Mol Cell Biol. 1998 June;18(6):3563-3571.
4.
FIG. 7

FIG. 7. From: XRCC1 Is Specifically Associated with Poly(ADP-Ribose) Polymerase and Negatively Regulates Its Activity following DNA Damage.

Network of interactions between enzymes and factors participating in the BER pathway. BRCT modules involved in PARP-XRCC1 and in DNA ligase III-XRCC1 (37) interactions are indicated. XRCC1 contacts DNA polymerase β (25) by its N-terminal region. PARP and DNA ligase III have the same nick detection motif (zinc finger F1 [F I], amino acids 1 to 97).

Murielle Masson, et al. Mol Cell Biol. 1998 June;18(6):3563-3571.
5.
FIG. 4

FIG. 4. From: XRCC1 Is Specifically Associated with Poly(ADP-Ribose) Polymerase and Negatively Regulates Its Activity following DNA Damage.

In vivo negative regulation of PARP activity by XRCC1. HeLa cells expressing either GST alone (A to C) or GST-XRCC1 (D to F) were treated with H2O2 for 10 min. After methanol-acetone fixation, the cells were incubated with a mixture of monoclonal antibodies against GST and against poly(ADP-ribose) (pADPr). The primary antibodies were detected with Texas red or fluorescein isothiocyanate-conjugated secondary antibodies. Arrowheads point out cells expressing GST-XRCC1 and lacking PARP activity (D to F). DAPI, 4′,6-diamidino-2-phenylindole.

Murielle Masson, et al. Mol Cell Biol. 1998 June;18(6):3563-3571.
6.
FIG. 3

FIG. 3. From: XRCC1 Is Specifically Associated with Poly(ADP-Ribose) Polymerase and Negatively Regulates Its Activity following DNA Damage.

Interaction of XRCC1 with GST-PARP and PARP functional domains. (A) Modular organization of PARP (diagram b) and truncated forms of PARP (diagrams c to g) expressed as GST-fusion proteins in HeLa cells. The asterisk indicates the BRCT motif present in domain D of PARP; FI and FII correspond to the PARP zinc fingers (4, 9). Fusion proteins and interacting endogenous proteins (XRCC1) were selectively extracted and analyzed by Western blotting as described in Materials and Methods with successively anti-GST (B) and anti-XRCC1 (C) antibodies. Lanes h and h′ contain total extract of control untransfected HeLa cells.

Murielle Masson, et al. Mol Cell Biol. 1998 June;18(6):3563-3571.
7.
FIG. 1

FIG. 1. From: XRCC1 Is Specifically Associated with Poly(ADP-Ribose) Polymerase and Negatively Regulates Its Activity following DNA Damage.

Interaction of PARP with GST-tagged XRCC1 domains. (A) Modular organization of XRCC1. Amino acids 84 to 183 make up the region that interacts with DNA polymerase (pol) β (25); amino acids 538 to 633 make up the region that interacts with DNA ligase III (37); amino acids 301 to 402 make up the region that interacts with PARP (cf. panels B and C); and amino acids 239 to 266 make up the NLS (cf. Fig. 2). The asterisks indicate the two BRCT modules (4, 9). The portion of XRCC1 encoded by the cDNA clone isolated in the two-hybrid procedure and the GST-tagged XRCC1 deletion mutants expressed in Cos-7 cells are also diagrammed. Expressed GST-fusion proteins and interacting endogenous proteins (PARP) were selectively extracted and analyzed by Western blotting as described in Materials and Methods with successively anti-GST (B) and anti-PARP (C) antibodies. Lanes a and a′ contain the total extract of control untransfected Cos-7 cells.

Murielle Masson, et al. Mol Cell Biol. 1998 June;18(6):3563-3571.

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