Saccharomyces cerevisiae Cmr1 protein preferentially binds to UV-damaged DNA in vitro

Choi, Do-Hee; Kwon, Sung-Hun; Kim, Joon-Ho; Bae, Sung‐Ho

doi:10.1007/s12275-012-1597-4

Cited by 16 publications

(31 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The role of these proteins in the DNA damage response is unclear since the deletion of any one gene does not result in a strong damage sensitivity phenotype. However, one member of this group, Cmr1, contributes to genome stability 32 and was recently demonstrated to interact with UV-damaged DNA in vitro and in vivo 52 . In one scenario, the chromatin remodeling activity of Hos2 might be required to permit Cmr1 to access ‘bulky’ DNA lesions.…”

Section: Discussionmentioning

confidence: 99%

Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress

et al. 2012

View full text Add to dashboard Cite

Re-localization of proteins is a hallmark of the DNA damage response. We use high-throughput microscopic screening of the yeast GFP fusion collection to develop a systems-level view of protein re-organization following drug-induced DNA replication stress. Changes in protein localization and abundance reveal drug-specific patterns of functional enrichments. Classification of proteins by sub-cellular destination allows the identification of pathways that respond to replication stress. We analyzed pairwise combinations of GFP fusions and gene deletion mutants to define and order two novel DNA damage responses. In the first, Cmr1 forms subnuclear foci that are regulated by the histone deacetylase Hos2 and are distinct from the typical Rad52 repair foci. In a second example, we find that the checkpoint kinases Mec1/Tel1 and the translation regulator Asc1 regulate P-body formation. This method identifies response pathways that were not detected in genetic and protein interaction screens, and can be readily applied to any form of chemical or genetic stress to reveal cellular response pathways.

show abstract

Section: Discussionmentioning

confidence: 99%

Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress

et al. 2012

View full text Add to dashboard Cite

show abstract

“…The Mte1-GFP fusion protein has been shown to form nuclear foci in response to replication stress Tkach et al 2012;Yimit et al 2015). Moreover, high-throughput screens have implicated Mte1 in telomere length maintenance (Askree et al 2004) and indicated that it can interact with Cmr1 (Gilmore et al 2012), a chromatin-binding protein associated with replication stress response (Choi et al 2012;Tkach et al 2012;Gallina et al 2015). In this report, we show that Mte1 is a D-loop-binding protein that interacts with the Mph1 helicase and has an antagonizing role to Mph1 in recombination outcomes by enhancing CO formation.…”

mentioning

confidence: 99%

Mte1 interacts with Mph1 and promotes crossover recombination and telomere maintenance

et al. 2016

View full text Add to dashboard Cite

Mph1 is a member of the conserved FANCM family of DNA motor proteins that play key roles in genome maintenance processes underlying Fanconi anemia, a cancer predisposition syndrome in humans. Here, we identify Mte1 as a novel interactor of the Mph1 helicase in Saccharomyces cerevisiae. In vitro, Mte1 (Mph1-associated telomere maintenance protein 1) binds directly to DNA with a preference for branched molecules such as D loops and fork structures. In addition, Mte1 stimulates the helicase and fork regression activities of Mph1 while inhibiting the ability of Mph1 to dissociate recombination intermediates. Deletion of MTE1 reduces crossover recombination and suppresses the sensitivity of mph1Δ mutant cells to replication stress. Mph1 and Mte1 interdependently colocalize at DNA damage-induced foci and dysfunctional telomeres, and MTE1 deletion results in elongated telomeres. Taken together, our data indicate that Mte1 plays a role in regulation of crossover recombination, response to replication stress, and telomere maintenance.

show abstract

Section: Introductionmentioning

confidence: 99%

“…Our experiment had begun before the availability of the newly revealed information about this gene in three recent studies that have investigated this gene [11–13]. Choi et al [11] used biochemical methods to find that the CMR1 gene's product binds the DNA and may be involved in DNA-damage responses. Gilmore et al [12] used integrative bioinformatics, quantitative proteomics and biochemical approaches to conclude that CMR1 is a member of the core histone network and is highly associated with the four histones as well as with many of the other proteins within the network.…”

Section: Introductionmentioning

confidence: 99%

Yeast gene CMR1/YDL156W is consistently co-expressed with genes participating in DNA-metabolic processes in a variety of stringent clustering experiments

Abu‐Jamous

Roberts

et al. 2013

J. R. Soc. Interface.

View full text Add to dashboard Cite

The binarization of consensus partition matrices (Bi-CoPaM) method has, among its unique features, the ability to perform ensemble clustering over the same set of genes from multiple microarray datasets by using various clustering methods in order to generate tunable tight clusters. Therefore, we have used the Bi-CoPaM method to the most synchronized 500 cell-cycle-regulated yeast genes from different microarray datasets to produce four tight, specific and exclusive clusters of co-expressed genes. We found 19 genes formed the tightest of the four clusters and this included the gene CMR1/YDL156W, which was an uncharacterized gene at the time of our investigations. Two very recent proteomic and biochemical studies have independently revealed many facets of CMR1 protein, although the precise functions of the protein remain to be elucidated. Our computational results complement these biological results and add more evidence to their recent findings of CMR1 as potentially participating in many of the DNA-metabolism processes such as replication, repair and transcription. Interestingly, our results demonstrate the close co-expressions of CMR1 and the replication protein A (RPA), the cohesion complex and the DNA polymerases α, δ and ɛ, as well as suggest functional relationships between CMR1 and the respective proteins. In addition, the analysis provides further substantial evidence that the expression of the CMR1 gene could be regulated by the MBF complex. In summary, the application of a novel analytic technique in large biological datasets has provided supporting evidence for a gene of previously unknown function, further hypotheses to test, and a more general demonstration of the value of sophisticated methods to explore new large datasets now so readily generated in biological experiments.

show abstract

Saccharomyces cerevisiae Cmr1 protein preferentially binds to UV-damaged DNA in vitro

Cited by 16 publications

References 22 publications

Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress

Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress

Mte1 interacts with Mph1 and promotes crossover recombination and telomere maintenance

Yeast gene CMR1/YDL156W is consistently co-expressed with genes participating in DNA-metabolic processes in a variety of stringent clustering experiments

Contact Info

Product

Resources

About