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  RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO

Hoege, C., Pfander, B., Moldovan, G. L., Pyrowolakis, G., & Jentsch, S. (2002). RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature, 419(6903), 135-141.

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Genre: Journal Article
Alternative Title : Nature

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 Creators:
Hoege, C.1, Author              
Pfander, B.2, Author              
Moldovan, G. L.1, Author              
Pyrowolakis, G.1, Author              
Jentsch, S.1, Author              
Affiliations:
1Jentsch, Stefan / Molecular Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565156              
2Pfander, Boris / DNA Replication and Genome Integrity, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565165              

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 Abstract: The RAD6 pathway is central to post-replicative DNA repair in eukaryotic cells; however, the machinery and its regulation remain poorly understood. Two principal elements of this pathway are the ubiquitin-conjugating enzymes RAD6 and the MMS2-UBC13 heterodimer, which are recruited to chromatin by the RING-finger proteins RAD18 and RAD5, respectively. Here we show that UBC9, a small ubiquitin-related modifier (SUMO)- conjugating enzyme, is also affiliated with this pathway and that proliferating cell nuclear antigen (PCNA)-a DNA-polymerase sliding clamp involved in DNA synthesis and repair-is a substrate. PCNA is monoubiquitinated through RAD6 and RAD18, modified by lysine-63-linked multi-ubiquitination-which additionally requires MMS2, UBC13 and RAD5-and is conjugated to SUMO by UBC9. All three modifications affect the same lysine residue of PCNA, suggesting that they label PCNA for alternative functions. We demonstrate that these modifications differentially affect resistance to DNA damage, and that damage-induced PCNA ubiquitination is elementary for DNA repair and occurs at the same conserved residue in yeast and humans.

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Language(s): eng - English
 Dates: 2002-09-12
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41639
ISI: 000177931200033
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Title: Nature
  Alternative Title : Nature
Source Genre: Journal
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Pages: - Volume / Issue: 419 (6903) Sequence Number: - Start / End Page: 135 - 141 Identifier: ISSN: 0028-0836