Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Published

Standard

Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis. / Bienko, Marzena; Green, Catherine M; Crosetto, Nicola et al.
In: Science, Vol. 310, No. 5755, 16.12.2005, p. 1821-4.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Bienko, M, Green, CM, Crosetto, N, Rudolf, F, Zapart, G, Coull, B, Kannouche, P, Wider, G, Peter, M, Lehmann, AR, Hofmann, K & Dikic, I 2005, 'Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis', Science, vol. 310, no. 5755, pp. 1821-4. https://doi.org/10.1126/science.1120615

APA

Bienko, M., Green, C. M., Crosetto, N., Rudolf, F., Zapart, G., Coull, B., Kannouche, P., Wider, G., Peter, M., Lehmann, A. R., Hofmann, K., & Dikic, I. (2005). Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis. Science, 310(5755), 1821-4. https://doi.org/10.1126/science.1120615

Vancouver

Bienko M, Green CM, Crosetto N, Rudolf F, Zapart G, Coull B et al. Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis. Science. 2005 Dec 16;310(5755):1821-4. doi: 10.1126/science.1120615

Author

Bienko, Marzena ; Green, Catherine M ; Crosetto, Nicola et al. / Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis. In: Science. 2005 ; Vol. 310, No. 5755. pp. 1821-4.

Bibtex

@article{6ef7e0e7562943ba8b394207d156b991,

title = "Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis",

abstract = "Translesion synthesis (TLS) is the major pathway by which mammalian cells replicate across DNA lesions. Upon DNA damage, ubiquitination of proliferating cell nuclear antigen (PCNA) induces bypass of the lesion by directing the replication machinery into the TLS pathway. Yet, how this modification is recognized and interpreted in the cell remains unclear. Here we describe the identification of two ubiquitin (Ub)-binding domains (UBM and UBZ), which are evolutionarily conserved in all Y-family TLS polymerases (pols). These domains are required for binding of poleta and poliota to ubiquitin, their accumulation in replication factories, and their interaction with monoubiquitinated PCNA. Moreover, the UBZ domain of poleta is essential to efficiently restore a normal response to ultraviolet irradiation in xeroderma pigmentosum variant (XP-V) fibroblasts. Our results indicate that Ub-binding domains of Y-family polymerases play crucial regulatory roles in TLS.",

keywords = "Amino Acid Motifs, Amino Acid Sequence, Animals, Cell Line, Computational Biology, DNA/biosynthesis, DNA Damage, DNA Repair, DNA Replication, DNA-Directed DNA Polymerase/chemistry, Humans, Hydrophobic and Hydrophilic Interactions, Models, Molecular, Molecular Sequence Data, Mutation, Nuclear Magnetic Resonance, Biomolecular, Point Mutation, Proliferating Cell Nuclear Antigen/metabolism, Protein Binding, Protein Conformation, Protein Interaction Mapping, Protein Structure, Tertiary, Recombinant Fusion Proteins/metabolism, Transfection, Ubiquitin/metabolism, Xeroderma Pigmentosum/genetics, Zinc Fingers",

author = "Marzena Bienko and Green, {Catherine M} and Nicola Crosetto and Fabian Rudolf and Grzegorz Zapart and Barry Coull and Patricia Kannouche and Gerhard Wider and Matthias Peter and Lehmann, {Alan R} and Kay Hofmann and Ivan Dikic",

year = "2005",

month = dec,

day = "16",

doi = "10.1126/science.1120615",

language = "English",

volume = "310",

pages = "1821--4",

journal = "Science",

issn = "0036-8075",

publisher = "American Association for the Advancement of Science",

number = "5755",

}

RIS

TY - JOUR

T1 - Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis

AU - Bienko, Marzena

AU - Green, Catherine M

AU - Crosetto, Nicola

AU - Rudolf, Fabian

AU - Zapart, Grzegorz

AU - Coull, Barry

AU - Kannouche, Patricia

AU - Wider, Gerhard

AU - Peter, Matthias

AU - Lehmann, Alan R

AU - Hofmann, Kay

AU - Dikic, Ivan

PY - 2005/12/16

Y1 - 2005/12/16

N2 - Translesion synthesis (TLS) is the major pathway by which mammalian cells replicate across DNA lesions. Upon DNA damage, ubiquitination of proliferating cell nuclear antigen (PCNA) induces bypass of the lesion by directing the replication machinery into the TLS pathway. Yet, how this modification is recognized and interpreted in the cell remains unclear. Here we describe the identification of two ubiquitin (Ub)-binding domains (UBM and UBZ), which are evolutionarily conserved in all Y-family TLS polymerases (pols). These domains are required for binding of poleta and poliota to ubiquitin, their accumulation in replication factories, and their interaction with monoubiquitinated PCNA. Moreover, the UBZ domain of poleta is essential to efficiently restore a normal response to ultraviolet irradiation in xeroderma pigmentosum variant (XP-V) fibroblasts. Our results indicate that Ub-binding domains of Y-family polymerases play crucial regulatory roles in TLS.

AB - Translesion synthesis (TLS) is the major pathway by which mammalian cells replicate across DNA lesions. Upon DNA damage, ubiquitination of proliferating cell nuclear antigen (PCNA) induces bypass of the lesion by directing the replication machinery into the TLS pathway. Yet, how this modification is recognized and interpreted in the cell remains unclear. Here we describe the identification of two ubiquitin (Ub)-binding domains (UBM and UBZ), which are evolutionarily conserved in all Y-family TLS polymerases (pols). These domains are required for binding of poleta and poliota to ubiquitin, their accumulation in replication factories, and their interaction with monoubiquitinated PCNA. Moreover, the UBZ domain of poleta is essential to efficiently restore a normal response to ultraviolet irradiation in xeroderma pigmentosum variant (XP-V) fibroblasts. Our results indicate that Ub-binding domains of Y-family polymerases play crucial regulatory roles in TLS.

KW - Amino Acid Motifs

KW - Amino Acid Sequence

KW - Animals

KW - Cell Line

KW - Computational Biology

KW - DNA/biosynthesis

KW - DNA Damage

KW - DNA Repair

KW - DNA Replication

KW - DNA-Directed DNA Polymerase/chemistry

KW - Humans

KW - Hydrophobic and Hydrophilic Interactions

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Mutation

KW - Nuclear Magnetic Resonance, Biomolecular

KW - Point Mutation

KW - Proliferating Cell Nuclear Antigen/metabolism

KW - Protein Binding

KW - Protein Conformation

KW - Protein Interaction Mapping

KW - Protein Structure, Tertiary

KW - Recombinant Fusion Proteins/metabolism

KW - Transfection

KW - Ubiquitin/metabolism

KW - Xeroderma Pigmentosum/genetics

KW - Zinc Fingers

U2 - 10.1126/science.1120615

DO - 10.1126/science.1120615

M3 - Journal article

C2 - 16357261

VL - 310

SP - 1821

EP - 1824

JO - Science

JF - Science

SN - 0036-8075

IS - 5755

ER -

Research

Links

Text available via DOI:

Keywords