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  The p12 subunit of human polymerase uses an atypical PIP box for molecular recognition of proliferating cell nuclear antigen (PCNA)

Gonzalez-Magana, A., Ibanez de Opakua, A., Romano-Moreno, M., Murciano-Calles, J., Merino, N., Luque, I., et al. (2019). The p12 subunit of human polymerase uses an atypical PIP box for molecular recognition of proliferating cell nuclear antigen (PCNA). Journal of Biological Chemistry, 294(11), 3947-3956. doi:10.1074/jbc.RA118.006391.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0003-4B09-0 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-4B0D-C
Genre: Journal Article

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 Creators:
Gonzalez-Magana, A., Author
Ibanez de Opakua, A.1, Author              
Romano-Moreno, M., Author
Murciano-Calles, J., Author
Merino, N., Author
Luque, I., Author
Rojas, A. L., Author
Onesti, S., Author
Blanco, F. J., Author
De Biasio, A., Author
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society, ou_578571              

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Free keywords: DNA replication; DNA polymerase; proliferating cell nuclear antigen (PCNA); protein-protein interaction; processivity; protein structure; PCNA interacting sequence; PIP-box
 Abstract: Human DNA polymerase is essential for DNA replication and acts in conjunction with the processivity factor proliferating cell nuclear antigen (PCNA). In addition to its catalytic subunit (p125), pol comprises three regulatory subunits (p50, p68, and p12). PCNA interacts with all of these subunits, but only the interaction with p68 has been structurally characterized. Here, we report solution NMR-, isothermal calorimetry-, and X-ray crystallography-based analyses of the p12-PCNA interaction, which takes part in the modulation of the rate and fidelity of DNA synthesis by pol . We show that p12 binds with micromolar affinity to the classical PIP-binding pocket of PCNA via a highly atypical PIP box located at the p12 N terminus. Unlike the canonical PIP box of p68, the PIP box of p12 lacks the conserved glutamine; binds through a 2-fork plug made of an isoleucine and a tyrosine residue at +3 and +8 positions, respectively; and is stabilized by an aspartate at +6 position, which creates a network of intramolecular hydrogen bonds. These findings add to growing evidence that PCNA can bind a diverse range of protein sequences that may be broadly grouped as PIP-like motifs as has been previously suggested.

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Language(s): eng - English
 Dates: 2019-01-172019-03-15
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1074/jbc.RA118.006391
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 294 (11) Sequence Number: - Start / End Page: 3947 - 3956 Identifier: -