Structure of p15PAF-PCNA complex and implications for clamp sliding during DNA replication and repair

Research output: Contribution to journal › Journal article › Research › peer-review

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Structure of p15PAF-PCNA complex and implications for clamp sliding during DNA replication and repair. / De Biasio, Alfredo; de Opakua, Alain Ibáñez; Mortuza, Gulnahar B; Molina, Rafael; Cordeiro, Tiago N; Castillo, Francisco; Villate, Maider; Merino, Nekane; Delgado, Sandra; Gil-Cartón, David; Luque, Irene; Diercks, Tammo; Bernadó, Pau; Montoya, Guillermo; Blanco, Francisco J.

In: Nature Communications, Vol. 6, 6439, 12.03.2015, p. 1-12.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

De Biasio, A, de Opakua, AI, Mortuza, GB, Molina, R, Cordeiro, TN, Castillo, F, Villate, M, Merino, N, Delgado, S, Gil-Cartón, D, Luque, I, Diercks, T, Bernadó, P, Montoya, G & Blanco, FJ 2015, 'Structure of p15PAF-PCNA complex and implications for clamp sliding during DNA replication and repair', Nature Communications, vol. 6, 6439, pp. 1-12. https://doi.org/10.1038/ncomms7439

APA

De Biasio, A., de Opakua, A. I., Mortuza, G. B., Molina, R., Cordeiro, T. N., Castillo, F., Villate, M., Merino, N., Delgado, S., Gil-Cartón, D., Luque, I., Diercks, T., Bernadó, P., Montoya, G., & Blanco, F. J. (2015). Structure of p15PAF-PCNA complex and implications for clamp sliding during DNA replication and repair. Nature Communications, 6, 1-12. [6439]. https://doi.org/10.1038/ncomms7439

Vancouver

De Biasio A, de Opakua AI, Mortuza GB, Molina R, Cordeiro TN, Castillo F et al. Structure of p15PAF-PCNA complex and implications for clamp sliding during DNA replication and repair. Nature Communications. 2015 Mar 12;6:1-12. 6439. https://doi.org/10.1038/ncomms7439

Author

De Biasio, Alfredo ; de Opakua, Alain Ibáñez ; Mortuza, Gulnahar B ; Molina, Rafael ; Cordeiro, Tiago N ; Castillo, Francisco ; Villate, Maider ; Merino, Nekane ; Delgado, Sandra ; Gil-Cartón, David ; Luque, Irene ; Diercks, Tammo ; Bernadó, Pau ; Montoya, Guillermo ; Blanco, Francisco J. / Structure of p15PAF-PCNA complex and implications for clamp sliding during DNA replication and repair. In: Nature Communications. 2015 ; Vol. 6. pp. 1-12.

Bibtex

@article{c4bf9196eb874821aec4941748452090,
title = "Structure of p15PAF-PCNA complex and implications for clamp sliding during DNA replication and repair",
abstract = "The intrinsically disordered protein p15(PAF) regulates DNA replication and repair by binding to the proliferating cell nuclear antigen (PCNA) sliding clamp. We present the structure of the human p15(PAF)-PCNA complex. Crystallography and NMR show the central PCNA-interacting protein motif (PIP-box) of p15(PAF) tightly bound to the front-face of PCNA. In contrast to other PCNA-interacting proteins, p15(PAF) also contacts the inside of, and passes through, the PCNA ring. The disordered p15(PAF) termini emerge at opposite faces of the ring, but remain protected from 20S proteasomal degradation. Both free and PCNA-bound p15(PAF) binds DNA mainly through its histone-like N-terminal tail, while PCNA does not, and a model of the ternary complex with DNA inside the PCNA ring is consistent with electron micrographs. We propose that p15(PAF) acts as a flexible drag that regulates PCNA sliding along the DNA and facilitates the switch from replicative to translesion synthesis polymerase binding.",
author = "{De Biasio}, Alfredo and {de Opakua}, {Alain Ib{\'a}{\~n}ez} and Mortuza, {Gulnahar B} and Rafael Molina and Cordeiro, {Tiago N} and Francisco Castillo and Maider Villate and Nekane Merino and Sandra Delgado and David Gil-Cart{\'o}n and Irene Luque and Tammo Diercks and Pau Bernad{\'o} and Guillermo Montoya and Blanco, {Francisco J}",
year = "2015",
month = mar,
day = "12",
doi = "10.1038/ncomms7439",
language = "English",
volume = "6",
pages = "1--12",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - Structure of p15PAF-PCNA complex and implications for clamp sliding during DNA replication and repair

AU - De Biasio, Alfredo

AU - de Opakua, Alain Ibáñez

AU - Mortuza, Gulnahar B

AU - Molina, Rafael

AU - Cordeiro, Tiago N

AU - Castillo, Francisco

AU - Villate, Maider

AU - Merino, Nekane

AU - Delgado, Sandra

AU - Gil-Cartón, David

AU - Luque, Irene

AU - Diercks, Tammo

AU - Bernadó, Pau

AU - Montoya, Guillermo

AU - Blanco, Francisco J

PY - 2015/3/12

Y1 - 2015/3/12

N2 - The intrinsically disordered protein p15(PAF) regulates DNA replication and repair by binding to the proliferating cell nuclear antigen (PCNA) sliding clamp. We present the structure of the human p15(PAF)-PCNA complex. Crystallography and NMR show the central PCNA-interacting protein motif (PIP-box) of p15(PAF) tightly bound to the front-face of PCNA. In contrast to other PCNA-interacting proteins, p15(PAF) also contacts the inside of, and passes through, the PCNA ring. The disordered p15(PAF) termini emerge at opposite faces of the ring, but remain protected from 20S proteasomal degradation. Both free and PCNA-bound p15(PAF) binds DNA mainly through its histone-like N-terminal tail, while PCNA does not, and a model of the ternary complex with DNA inside the PCNA ring is consistent with electron micrographs. We propose that p15(PAF) acts as a flexible drag that regulates PCNA sliding along the DNA and facilitates the switch from replicative to translesion synthesis polymerase binding.

AB - The intrinsically disordered protein p15(PAF) regulates DNA replication and repair by binding to the proliferating cell nuclear antigen (PCNA) sliding clamp. We present the structure of the human p15(PAF)-PCNA complex. Crystallography and NMR show the central PCNA-interacting protein motif (PIP-box) of p15(PAF) tightly bound to the front-face of PCNA. In contrast to other PCNA-interacting proteins, p15(PAF) also contacts the inside of, and passes through, the PCNA ring. The disordered p15(PAF) termini emerge at opposite faces of the ring, but remain protected from 20S proteasomal degradation. Both free and PCNA-bound p15(PAF) binds DNA mainly through its histone-like N-terminal tail, while PCNA does not, and a model of the ternary complex with DNA inside the PCNA ring is consistent with electron micrographs. We propose that p15(PAF) acts as a flexible drag that regulates PCNA sliding along the DNA and facilitates the switch from replicative to translesion synthesis polymerase binding.

U2 - 10.1038/ncomms7439

DO - 10.1038/ncomms7439

M3 - Journal article

C2 - 25762514

VL - 6

SP - 1

EP - 12

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 6439

ER -

ID: 140241975