| Functional studies show that Rtt107 binding of partner proteins of diverse activities promotes genome replication and stability in both distinct and concerted manners. A unified theme is that tetra- and di-BRCT domains of Rtt107 collaborate to recruit partner proteins to chromatin | Molecular Basis for Control of Diverse Genome Stability Factors by the Multi-BRCT Scaffold Rtt107.
Wan B, Wu J, Meng X, Lei M, Zhao X., Free PMC Article | 01/25/2020 |
| Rtt107 prevents checkpoint hyperactivation after replicative stress by limiting DNA damage | Budding yeast Rtt107 prevents checkpoint hyperactivation after replicative stress by limiting DNA damage.
Brown JAR, Kobor MS. | 07/20/2019 |
| The scaffold protein Rtt107, which binds the Mus81-Mms4 complex, interacts with Cdc7 and thereby targets Cdc7-Dbf4 and Cdc5 to the complex enabling full Mus81 activation. | Dbf4-dependent kinase and the Rtt107 scaffold promote Mus81-Mms4 resolvase activation during mitosis.
Princz LN, Wild P, Bittmann J, Aguado FJ, Blanco MG, Matos J, Pfander B., Free PMC Article | 07/8/2017 |
| A key function of the Rtt107 BRCT domains for targeting of both itself and its interaction partners to DNA lesions was revealed. | Rtt107 BRCT domains act as a targeting module in the DNA damage response.
Leung GP, Brown JA, Glover JN, Kobor MS. | 11/5/2016 |
| Slx4 and Rtt107 control checkpoint signalling and DNA resection at double-strand breaks. | Slx4 and Rtt107 control checkpoint signalling and DNA resection at double-strand breaks.
Dibitetto D, Ferrari M, Rawal CC, Balint A, Kim T, Zhang Z, Smolka MB, Brown GW, Marini F, Pellicioli A., Free PMC Article | 06/28/2016 |
| Rtt107 is a multi-functional scaffold supporting replication progression with partners SUMO, ubiquitin ligase E3, and SLX4. | Rtt107 Is a Multi-functional Scaffold Supporting Replication Progression with Partner SUMO and Ubiquitin Ligases.
Hang LE, Peng J, Tan W, Szakal B, Menolfi D, Sheng Z, Lobachev K, Branzei D, Feng W, Zhao X., Free PMC Article | 01/30/2016 |
| The DNA repair scaffold proteins Slx4 and Rtt107 utilize a minimal multi-BRCT-domain module for phosphatase-independent downregulation of DNA damage response signals in yeast. | Dampening DNA damage checkpoint signalling via coordinated BRCT domain interactions.
Cussiol JR, Jablonowski CM, Yimit A, Brown GW, Smolka MB., Free PMC Article | 08/29/2015 |
| The C-terminal tandem BRCT repeats of Rtt107 interaction with gammaH2A is functionally important during DNA repair. | Structure of C-terminal tandem BRCT repeats of Rtt107 protein reveals critical role in interaction with phosphorylated histone H2A during DNA damage repair.
Li X, Liu K, Li F, Wang J, Huang H, Wu J, Shi Y., Free PMC Article | 06/16/2012 |
| a multifaceted functional relationship between Rtt107 and Dot1 in the DNA damage response and maintenance of genome integrity. | Loss of H3 K79 trimethylation leads to suppression of Rtt107-dependent DNA damage sensitivity through the translesion synthesis pathway.
Lévesque N, Leung GP, Fok AK, Schmidt TI, Kobor MS., Free PMC Article | 12/4/2010 |
| Multiple fork repair factors associate with Rtt107 or Slx4, supporting that Mec1-dependent assembly of the Rtt107-Slx4-Dpb11 complex functions to coordinate fork repair. | DNA damage signaling recruits the Rtt107-Slx4 scaffolds via Dpb11 to mediate replication stress response.
Ohouo PY, Bastos de Oliveira FM, Almeida BS, Smolka MB. | 08/23/2010 |
| Slx4-dependent phosphorylation of Rtt107 by Mec1 is critical for replication restart after alkylation damage. | Slx4 regulates DNA damage checkpoint-dependent phosphorylation of the BRCT domain protein Rtt107/Esc4.
Roberts TM, Kobor MS, Bastin-Shanower SA, Ii M, Horte SA, Gin JW, Emili A, Rine J, Brill SJ, Brown GW., Free PMC Article | 01/21/2010 |
| Esc4 binds the Rad55/Rad56 heterodimer and forms subnuclear foci in response to DNA damage that stalls replication forks. | Esc4/Rtt107 and the control of recombination during replication.
Chin JK, Bashkirov VI, Heyer WD, Romesberg FE., Free PMC Article | 01/21/2010 |
| These results indicate that Rtt109, Rtt101, and Rtt107, which genetic evidence suggests are functionally related, form a DNA damage response pathway that recruits Rtt107 complexes to damaged or stalled replication forks. | Regulation of rtt107 recruitment to stalled DNA replication forks by the cullin rtt101 and the rtt109 acetyltransferase.
Roberts TM, Zaidi IW, Vaisica JA, Peter M, Brown GW, Roberts TM, Zaidi IW, Vaisica JA, Peter M, Brown GW., Free PMC Articles: PMC2174167, PMC2174167 | 01/21/2010 |
| Rtt107 is recruited to chromatin following DNA damage that stalls DNA replication forks. This recruitment depends on the acetyltransferase Rtt109 and the cullin Rtt101. Chromatin-bound Rtt107 is localized at or near stalled replication forks. | Regulation of rtt107 recruitment to stalled DNA replication forks by the cullin rtt101 and the rtt109 acetyltransferase.
Roberts TM, Zaidi IW, Vaisica JA, Peter M, Brown GW, Roberts TM, Zaidi IW, Vaisica JA, Peter M, Brown GW., Free PMC Articles: PMC2174167, PMC2174167 | 10/21/2008 |
| identify Esc4p as an important new S-phase-specific target of monitors and participates in meiotic recombination Mec1p | Esc4p, a new target of Mec1p (ATR), promotes resumption of DNA synthesis after DNA damage.
Rouse J., Free PMC Article | 01/21/2010 |