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Roberts syndrome

Baoshan Xu, Shuai Lu, Jennifer L Gerton
2014 Rare Diseases  
Following microinjection, embryos were incubated with 4 mM L-glutamine plus either 10 mM d-leucine, which is biologically inactive, or 10 mM l-leucine for 2 d post fertilization (dpf) and then photographed  ...  This leads to global changes in gene expression and cell physiology 47 (Xu and Gerton, unpublished) . mTORC1 is a protein kinase that senses cellular stress, such as amino acid deprivation, and responds  ... 
doi:10.4161/rdis.27743 pmid:25054091 pmcid:PMC4091327 fatcat:aoscgxqrzjbx3nh427q5ytik2u

Mammalian oogenesis and female reproductive aging

Francesca E. Duncan, Jennifer L. Gerton
2018 Aging  
doi:10.18632/aging.101381 pmid:29410392 pmcid:PMC5842846 fatcat:7ksw7fks4vhjra7da3dfsfxerq

Translational mechanisms at work in the cohesinopathies

Jennifer L. Gerton
2012 Nucleus  
In 2004 came the first reports associating mutations in a cohesin Translational mechanisms at work in the cohesinopathies Jennifer L.  ...  Gerton The Stowers Institute for Medical Research; Kansas City, MO USA loading factor, NIPBL, with human disease.  ... 
doi:10.4161/nucl.22800 pmid:23138777 pmcid:PMC3515535 fatcat:q6wlwa5jrfcaxn4soypfogmx34

The SMC loader Scc2 regulates gene expression

Musinu Zakari, Jennifer L Gerton
2015 Cell Cycle  
Comment on: Lindgren E, et al. Inactivation of the budding yeast cohesin loader Scc2 alters gene expression both globally and in response to a single DNA double strand break. Cell cycle 2014; 13(23):3645-58; http://dx.
doi:10.1080/15384101.2015.1010959 pmid:25715109 pmcid:PMC4613598 fatcat:awrdcvikpvhydlc327vgtrgug4

Taking cohesin and condensin in context

Kobe C. Yuen, Jennifer L. Gerton, Mónica P. Colaiácovo
2018 PLoS Genetics  
Carriere L, Graziani S, Alibert O, Ghavi-Helm Y, Boussouar F, Humbertclaude H, et al.  ...  Yuen KC, Slaughter BD, Gerton JL. Condensin II is anchored by TFIIIC and H3K4me3 in the mamma- lian genome and supports the expression of active dense gene clusters.  ... 
doi:10.1371/journal.pgen.1007118 pmid:29370184 pmcid:PMC5784890 fatcat:3ji3w5uubvdpvaye6heatdthx4

A transcription factor primes the condensin pump

Jennifer L. Gerton
2018 Journal of Cell Biology  
Gerton is supported by the Stowers Institute for Medical Research. The author declares no competing financial interests.  ... 
doi:10.1083/jcb.201806043 pmid:29925630 fatcat:emlid23f3nhxtei2ki3m3fzmpq

Cohesinopathies, gene expression, and chromatin organization

Tania Bose, Jennifer L. Gerton
2010 Journal of Cell Biology  
Many additional proteins are part of the co hesin network (for review see Xiong and Gerton, 2010) .  ... 
doi:10.1083/jcb.200912129 pmid:20404106 pmcid:PMC2856913 fatcat:itabqdfdbfgm3o74scot27v4ja

Ribosomal DNA-connecting ribosome biogenesis and chromosome biology

Lev Porokhovnik, Jennifer L. Gerton
2019 Chromosome Research  
A review article from Tamara Potapova and Jennifer Gerton addresses the proteins and models for organization of ribosomal DNA into nucleoli.  ...  The repair, stability, and adaptability of the ribosomal DNA is addressed by two reviews, one by Daniel Warmerdam and Rob Wolthuis and one by Devika Salim and Jennifer Gerton.  ... 
doi:10.1007/s10577-018-9601-4 fatcat:4rgarrelkzgbvgv6k3jgngwsjy

Improved transcription and translation with L-leucine stimulation of mTORC1 in Roberts syndrome

Baoshan Xu, Madelaine Gogol, Karin Gaudenz, Jennifer L. Gerton
2016 BMC Genomics  
Results: In this study, we use RBS cells to model mTORC1 repression and analyze transcription and translation with ribosome profiling to determine gene-level effects of L-leucine.  ...  Treatment of RBS cells and zebrafish RBS models with L-leucine partially rescued mTOR function and protein synthesis, correlating with increased cell division and improved development.  ...  L) for 3 or 24 h.  ... 
doi:10.1186/s12864-015-2354-y pmid:26729373 pmcid:PMC4700579 fatcat:llof57hrxvhjdpsf5ag2pymaoi

Etiology and pathogenesis of the cohesinopathies

Musinu Zakari, Kobe Yuen, Jennifer L. Gerton
2015 Wiley Interdisciplinary Reviews: Developmental Biology  
The reduced TOR activity in the cohesinopathies makes them a good candidate for treatment with the TOR stimulator l-leucine. 55, 89 Despite the fact that cohesinopathies and ribosomopathies share overlapping  ... 
doi:10.1002/wdev.190 pmid:25847322 fatcat:o36oxuf24nhxbcabwzcwmgxece

Scm3 Is a Centromeric Nucleosome Assembly Factor

Manjunatha Shivaraju, Raymond Camahort, Mark Mattingly, Jennifer L. Gerton
2011 Journal of Biological Chemistry  
The Cse4 nucleosome at each budding yeast centromere must be faithfully assembled each cell cycle to specify the site of kinetochore assembly and microtubule attachment for chromosome segregation. Although Scm3 is required for the localization of the centromeric H3 histone variant Cse4 to centromeres, its role in nucleosome assembly has not been tested. We demonstrate that Scm3 is able to mediate the assembly of Cse4 nucleosomes in vitro, but not H3 nucleosomes, as measured by a supercoiling
more » ... ay. Localization of Cse4 to centromeres and the assembly activity depend on an evolutionarily conserved core motif in Scm3, but localization of the CBF3 subunit Ndc10 to centromeres does not depend on this motif. The centromere targeting domain of Cse4 is sufficient for Scm3 nucleosome assembly activity. Assembly does not depend on centromeric sequence. We propose that Scm3 plays an active role in centromeric nucleosome assembly.
doi:10.1074/jbc.m110.183640 pmid:21317428 pmcid:PMC3069404 fatcat:drnmfvdjxvgltlclkbzzlqcmbi

Protocol for mouse trophoblast stem cell isolation, differentiation, and cytokine detection

Vijay Pratap Singh, Jennifer L. Gerton
2021 STAR Protocols  
We thank members of the Gerton lab at the Stowers Institute for discussions. We thank Heidi Monnin and Maria Katt for technical support.  ... 
doi:10.1016/j.xpro.2020.100242 pmid:33458704 pmcid:PMC7797921 fatcat:tfqspjsm3jajdl34aydgc5mowq

Cohesin and human disease: lessons from mouse models

Vijay Pratap Singh, Jennifer L Gerton
2015 Current Opinion in Cell Biology  
The aneuploidy is not due to a Cohesin and human disease: lessons from mouse models Singh and Gerton 11 Source: Adapted from Ref.  ... 
doi:10.1016/j.ceb.2015.08.003 pmid:26343989 fatcat:e5plkch5dfc5dmnmuilkwsbvh4

Stimulation of mTORC1 with L-leucine Rescues Defects Associated with Roberts Syndrome

Baoshan Xu, Kenneth K. Lee, Lily Zhang, Jennifer L. Gerton, Nancy B. Spinner
2013 PLoS Genetics  
Stimulation of the TOR pathway with L-leucine rescued many developmental defects of ESCO2-mutant embryos.  ...  We thank Paul Trainor, Julia Horsfield, and Gerton lab members for helpful discussions. We thank Benjamin Ebert for sharing unpublished data. Author Contributions  ...  To further test the cooperative effects of L-Glu and L-Leu, ESCO2morphants were treated with L-Glu alone or L-Leu alone.  ... 
doi:10.1371/journal.pgen.1003857 pmid:24098154 pmcid:PMC3789817 fatcat:xfqhvmtxdje2rp6fmtpmt5cqsa

Hos1 Is a Lysine Deacetylase for the Smc3 Subunit of Cohesin

Bo Xiong, Shuai Lu, Jennifer L. Gerton
2010 Current Biology  
Chromosome cohesion is a cell-cycle-regulated process in which sister chromatids are held together from the time of replication until the time of separation at the metaphaseto-anaphase transition, ensuring accurate chromosome segregation [1] [2] [3] [4] [5] [6] [7] [8] [9] . Chromosome cohesion is established during S phase, and this process requires the four subunits of the cohesin complex (Smc1, Smc3, Mcd1/Scc1, and Irr1/ Scc3) and the acetyltransferase Eco1 [10] [11] [12] [13] . Acetylation
more » ... f Smc3 by Eco1 at two evolutionarily conserved lysine residues promotes cohesion establishment during S phase in budding yeast and humans [14] [15] [16] . Here we report that Hos1, a member of the evolutionarily conserved class I histone deacetylase family, acts as a deacetylase for Smc3 in S. cerevisiae. We examine the Smc3 acetylation level in nine histone deacetylase deletion strains and find that the acetylation level is increased specifically in a hos1D strain post-S phase. Coimmunoprecipitation experiments show that Hos1 interacts with Smc3 and that the interaction is most pronounced as cells reach anaphase. We provide direct evidence that Hos1 can deacetylate Smc3 and retains a soluble pool of deacetylated Smc3. Overexpression of Hos1 results in less acetylation of Smc3 and cohesion defects in both WT and eco1 mutant strains; mutation of the Hos1 active site abolishes the defects. Hos1 may help to maintain a pool of unacetylated Smc3 that can be used for new chromosome cohesion. Results and Discussion Identification of a Deacetylase for Smc3 Reversible acetylation of histone and non-histone proteins by HATs (histone acetyltransferases) and HDACs (histone deacetylases) has been increasingly reported to regulate many cellular processes, including gene transcription; DNA replication, repair, and recombination; metabolism; cytoskeletal dynamics; apoptosis; protein folding; and cellular signaling [17] [18] [19] [20] [21] . Because the establishment of chromosome cohesion depends on Smc3 acetylation by the acetyltransferase Eco1, it is reasonable to speculate that a deacetylase for Smc3 might exist. In budding yeast, ten known histone deacetylases have been identified and divided into three main classes (I, II, and III) on the basis of sequence homology [22, 23] . Class I and II deacetylases use zinc-dependent catalysis, whereas class III deacetylases are NAD+ dependent. To examine whether one of the histone deacetylases is responsible for Smc3 deacetylation, we immunoprecipitated the cohesin complex from extracts of deacetylase deletion strains and then examined the Smc3 acetylation level by using anti-acetyl-lysine antibody. As shown in Figure 1A , the Smc3 acetylation level in a hos1D strain was significantly increased over that in wild-type and other deacetylase deletion strains, suggesting that Hos1 is a potential candidate for an Smc3 deacetylase. Because Smc3 acetylation by Eco1 occurs during S phase, we asked in which phase of the cell cycle Hos1 exerts its function. The cohesin complex was immunoprecipitated from a culture arrested in G1 and at various times after release for both wild-type and hos1D strains, and Smc3 acetylation was analyzed. In G1 cells, Smc3 acetylation was not detectable in either wild-type or a hos1D strain; no Smc3 was pulled down because of the instability of Mcd1 at this time. Once cells entered S phase, Smc3 acetylation could be observed. At time points following DNA replication (45, 60, and 80 min after release), the level of Smc3 acetylation was clearly higher in a hos1D strain than in the wild-type, suggesting Hos1 might normally function after S phase ( Figure 1B) . We further investigated whether acetylation was affected in the chromatinbound fraction (the cohesive fraction) of Smc3 or the soluble fraction. Although acetylated Smc3 clearly increases in the hos1D strain in the chromatin-bound fraction, what is more striking is the presence of acetylated Smc3 in the soluble fraction ( Figure 1C ). These results suggest that acetylation of Smc3, and particularly soluble Smc3, is regulated by Hos1 after S phase. Hos1 Interacts with Smc3 in a Cell-Cycle-Dependent Manner Given that Hos1 regulates acetylation of Smc3, we tested for an interaction between Hos1 and Smc3. An interaction between Hos1 and Smc3 can be detected in an asynchronous culture ( Figure 2A ). Because Smc3 deacetylation by Hos1 is cell-cycle regulated, we examined the interaction over the cell cycle. Coimmunoprecipitation (co-IP) was carried out from whole-cell extracts in a G1 release experiment similar to that in Figure 1 in the epitope-tagged strains, and immunoblotting was then performed. The interaction between Hos1 and Smc3 was most strongly detected in cells with 2N DNA content ( Figure 2B) , consistent with the idea that Hos1 might act on Smc3 after S phase. We stained the nuclei from the 60 and 80 min time point with DAPI to determine whether the cells contained one or two DAPI masses, indicative of metaphase or anaphase, respectively. At the 60 min time point, 17% of cells had two DAPI masses, and 44% had two DAPI masses at the 80 min time point. These results suggest that the interaction between Smc3 and Hos1 is increasing as the cells progress to anaphase.
doi:10.1016/j.cub.2010.08.019 pmid:20797861 fatcat:4k2lkikrijay7dbip2nw5sak6m
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