Rtt101 and Mms1 in budding yeast form a CUL4(DDB1)-like ubiquitin ligase that promotes replication through damaged DNA

Research output: Contribution to journalArticle

Standard

Rtt101 and Mms1 in budding yeast form a CUL4(DDB1)-like ubiquitin ligase that promotes replication through damaged DNA. / Zaidi, Iram Waris; Rabut, Gwénaël; Poveda, Ana; Scheel, Hartmut; Malmström, Johan; Ulrich, Helle; Hofmann, Kay; Pasero, Philippe; Peter, Matthias; Luke, Brian.

In: EMBO Reports, Vol. 9, No. 10, 10.2008, p. 1034-40.

Research output: Contribution to journalArticle

Harvard

Zaidi, IW, Rabut, G, Poveda, A, Scheel, H, Malmström, J, Ulrich, H, Hofmann, K, Pasero, P, Peter, M & Luke, B 2008, 'Rtt101 and Mms1 in budding yeast form a CUL4(DDB1)-like ubiquitin ligase that promotes replication through damaged DNA', EMBO Reports, vol. 9, no. 10, pp. 1034-40. https://doi.org/10.1038/embor.2008.155

APA

CBE

MLA

Vancouver

Author

Zaidi, Iram Waris ; Rabut, Gwénaël ; Poveda, Ana ; Scheel, Hartmut ; Malmström, Johan ; Ulrich, Helle ; Hofmann, Kay ; Pasero, Philippe ; Peter, Matthias ; Luke, Brian. / Rtt101 and Mms1 in budding yeast form a CUL4(DDB1)-like ubiquitin ligase that promotes replication through damaged DNA. In: EMBO Reports. 2008 ; Vol. 9, No. 10. pp. 1034-40.

RIS

TY - JOUR

T1 - Rtt101 and Mms1 in budding yeast form a CUL4(DDB1)-like ubiquitin ligase that promotes replication through damaged DNA

AU - Zaidi, Iram Waris

AU - Rabut, Gwénaël

AU - Poveda, Ana

AU - Scheel, Hartmut

AU - Malmström, Johan

AU - Ulrich, Helle

AU - Hofmann, Kay

AU - Pasero, Philippe

AU - Peter, Matthias

AU - Luke, Brian

PY - 2008/10

Y1 - 2008/10

N2 - In budding yeast the cullin Rtt101 promotes replication fork progression through natural pause sites and areas of DNA damage, but its relevant subunits and molecular mechanism remain poorly understood. Here, we show that in budding yeast Mms1 and Mms22 are functional subunits of an Rtt101-based ubiquitin ligase that associates with the conjugating-enzyme Cdc34. Replication forks in mms1Delta, mms22Delta and rtt101Delta cells are sensitive to collisions with drug-induced DNA lesions, but not to transient pausing induced by nucleotide depletion. Interaction studies and sequence analysis have shown that Mms1 resembles human DDB1, suggesting that Rtt101(Mms1) is the budding yeast counterpart of the mammalian CUL4(DDB1) ubiquitin ligase family. Rtt101 interacts in an Mms1-dependent manner with the putative substrate-specific adaptors Mms22 and Crt10, the latter being a regulator of expression of ribonucleotide reductase. Taken together, our data suggest that the Rtt101(Mms1) ubiquitin ligase complex might be required to reorganize replication forks that encounter DNA lesions.

AB - In budding yeast the cullin Rtt101 promotes replication fork progression through natural pause sites and areas of DNA damage, but its relevant subunits and molecular mechanism remain poorly understood. Here, we show that in budding yeast Mms1 and Mms22 are functional subunits of an Rtt101-based ubiquitin ligase that associates with the conjugating-enzyme Cdc34. Replication forks in mms1Delta, mms22Delta and rtt101Delta cells are sensitive to collisions with drug-induced DNA lesions, but not to transient pausing induced by nucleotide depletion. Interaction studies and sequence analysis have shown that Mms1 resembles human DDB1, suggesting that Rtt101(Mms1) is the budding yeast counterpart of the mammalian CUL4(DDB1) ubiquitin ligase family. Rtt101 interacts in an Mms1-dependent manner with the putative substrate-specific adaptors Mms22 and Crt10, the latter being a regulator of expression of ribonucleotide reductase. Taken together, our data suggest that the Rtt101(Mms1) ubiquitin ligase complex might be required to reorganize replication forks that encounter DNA lesions.

KW - Anaphase-Promoting Complex-Cyclosome

KW - Cullin Proteins

KW - DNA Damage

KW - DNA Replication

KW - DNA-Binding Proteins

KW - Humans

KW - Protein Subunits

KW - Saccharomyces cerevisiae

KW - Saccharomyces cerevisiae Proteins

KW - Ubiquitin-Conjugating Enzymes

KW - Ubiquitin-Protein Ligase Complexes

KW - Ubiquitin-Protein Ligases

KW - Comparative Study

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1038/embor.2008.155

DO - 10.1038/embor.2008.155

M3 - Article

VL - 9

SP - 1034

EP - 1040

JO - EMBO Reports

T2 - EMBO Reports

JF - EMBO Reports

SN - 1469-221X

IS - 10

ER -