Database : MEDLINE
Search on : Ring and Chromosomes [Words]
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[PMID]: 29514846
[Au] Autor:Das A; Cesario J; Hinman AM; Jang JK; McKim KS
[Ad] Address:Rutgers University.
[Ti] Title:Kinesin 6 Regulation in Female Meiosis by the Non-conserved N- and C-Terminal Domains.
[So] Source:G3 (Bethesda);, 2018 Mar 09.
[Is] ISSN:2160-1836
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Bipolar spindle assembly occurs in the absence of centrosomes in the oocytes of most organisms. In the absence of centrosomes in oocytes, we have proposed that the kinesin 6 Subito, a MKLP-2 homolog, is required for establishing spindle bipolarity and chromosome biorientation by assembling a robust central spindle during prometaphase I. Although the functions of the conserved motor domains of kinesins is well studied, less is known about the contribution of the poorly conserved N- and C- terminal domains to motor function. In this study, we have investigated the contribution of these domains to kinesin 6 functions in meiosis and early embryonic development. We found that the N-terminal domain has antagonistic elements that regulate localization of the motor to microtubules. Other parts of the N- and C- terminal domains are not required for microtubule localization but are required for motor function. Some of these elements of Subito are more important for either mitosis or meiosis, as revealed by separation-of-function mutants. One of the functions for both the N- and C-terminals domains is to restrict the CPC to the central spindle in a ring around the chromosomes. We also provide evidence that CDK1 phosphorylation of Subito regulates its activity associated with homolog bi-orientation. These results suggest the N- and C-terminal domains of Subito, while not required for localization to the central spindle microtubules, have important roles regulating Subito, by interacting with other spindle proteins and promoting activities such as bipolar spindle formation and homologous chromosome bi-orientation during meiosis.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

  2 / 3523 MEDLINE  
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[PMID]: 29311228
[Au] Autor:Mangal S; Sacher J; Kim T; Osório DS; Motegi F; Carvalho AX; Oegema K; Zanin E
[Ad] Address:Center for Integrated Protein Science, Department Biology II, Ludwig-Maximilians University Munich, Planegg-Martinsried, Germany.
[Ti] Title:TPXL-1 activates Aurora A to clear contractile ring components from the polar cortex during cytokinesis.
[So] Source:J Cell Biol;217(3):837-848, 2018 Mar 05.
[Is] ISSN:1540-8140
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:During cytokinesis, a signal from the central spindle that forms between the separating anaphase chromosomes promotes the accumulation of contractile ring components at the cell equator, while a signal from the centrosomal microtubule asters inhibits accumulation of contractile ring components at the cell poles. However, the molecular identity of the inhibitory signal has remained unknown. To identify molecular components of the aster-based inhibitory signal, we developed a means to monitor the removal of contractile ring proteins from the polar cortex after anaphase onset. Using this assay, we show that polar clearing is an active process that requires activation of Aurora A kinase by TPXL-1. TPXL-1 concentrates on astral microtubules coincident with polar clearing in anaphase, and its ability to recruit Aurora A and activate its kinase activity are essential for clearing. In summary, our data identify Aurora A kinase as an aster-based inhibitory signal that restricts contractile ring components to the cell equator during cytokinesis.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:In-Data-Review
[do] DOI:10.1083/jcb.201706021

  3 / 3523 MEDLINE  
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[PMID]: 29521627
[Au] Autor:Zhang L; Köhler S; Rillo-Bohn R; Dernburg AF
[Ad] Address:Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.
[Ti] Title:A compartmentalized signaling network mediates crossover control in meiosis.
[So] Source:Elife;7, 2018 Mar 09.
[Is] ISSN:2050-084X
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:During meiosis, each pair of homologous chromosomes typically undergoes at least one crossover (crossover assurance), but these exchanges are strictly limited in number and widely spaced along chromosomes (crossover interference). The molecular basis for this chromosome-wide regulation remains mysterious. A family of meiotic RING finger proteins has been implicated in crossover regulation across eukaryotes. expresses four such proteins, of which one (ZHP-3) is known to be required for crossovers. Here we investigate the functions of ZHP-1, ZHP-2, and ZHP-4. We find that all four ZHP proteins, like their homologs in other species, localize to the synaptonemal complex, an unusual, liquid crystalline compartment that assembles between paired homologs. Together they promote accumulation of pro-crossover factors, including ZHP-3 and ZHP-4, at a single recombination intermediate, thereby patterning exchanges along each chromosome. These proteins also act at the top of a hierarchical, symmetry-breaking process that enables crossovers to direct accurate chromosome segregation.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:Publisher

  4 / 3523 MEDLINE  
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[PMID]: 29331044
[Au] Autor:Sharma A; Tiwari M; Gupta A; Pandey AN; Yadav PK; Chaube SK
[Ad] Address:Cell Physiology Laboratory, Department of Zoology, Institute of Science, Banaras Hindu University, Varanasi, India.
[Ti] Title:Journey of oocyte from metaphase-I to metaphase-II stage in mammals.
[So] Source:J Cell Physiol;, 2018 Jan 13.
[Is] ISSN:1097-4652
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:In mammals, journey from metaphase-I (M-I) to metaphase-II (M-II) is important since oocyte extrude first polar body (PB-I) and gets converted into haploid gamete. The molecular and cellular changes associated with meiotic cell cycle progression from M-I to M-II stage and extrusion of PB-I remain ill understood. Several factors drive oocyte meiosis from M-I to M-II stage. The mitogen-activated protein kinase3/1 (MAPK3/1), signal molecules and Rho family GTPases act through various pathways to drive cell cycle progression from M-I to M-II stage. The down regulation of MOS/MEK/MAPK3/1 pathway results in the activation of anaphase-promoting complex/cyclosome (APC/C). The active APC/C destabilizes maturation promoting factor (MPF) and induces meiotic resumption. Several signal molecules such as, c-Jun N-terminal kinase (JNK2), SENP3, mitotic kinesin-like protein 2 (MKlp2), regulator of G-protein signaling (RGS2), Epsin2, polo-like kinase 1 (Plk1) are directly or indirectly involved in chromosomal segregation. Rho family GTPase is another enzyme that along with cell division cycle (Cdc42) to form actomyosin contractile ring required for chromosomal segregation. In the presence of origin recognition complex (ORC4), eccentrically localized haploid set of chromosomes trigger cortex differentiation and determine the division site for polar body formation. The actomyosin contractile activity at the site of division plane helps to form cytokinetic furrow that results in the formation and extrusion of PB-I. Indeed, oocyte journey from M-I to M-II stage is coordinated by several factors and pathways that enable oocyte to extrude PB-I. Quality of oocyte directly impact fertilization rate, early embryonic development, and reproductive outcome in mammals.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180306
[Lr] Last revision date:180306
[St] Status:Publisher
[do] DOI:10.1002/jcp.26467

  5 / 3523 MEDLINE  
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[PMID]: 29467491
[Au] Autor:L Abbate A; Tolomeo D; Cifola I; Severgnini M; Turchiano A; Augello B; Squeo G; D Addabbo P; Traversa D; Daniele G; Lonoce A; Pafundi M; Carella M; Palumbo O; Dolnik A; Muehlematter D; Schoumans J; Van Roy N; De Bellis G; Martinelli G; Merla G; Bullinger L; Haferlach C; Storlazzi CT
[Ad] Address:Department of Biology, University of Bari "Aldo Moro", Bari, Italy.
[Ti] Title:MYC-containing amplicons in acute myeloid leukemia: genomic structures, evolution, and transcriptional consequences.
[So] Source:Leukemia;, 2018 Feb 22.
[Is] ISSN:1476-5551
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Double minutes (dmin), homogeneously staining regions, and ring chromosomes are vehicles of gene amplification in cancer. The underlying mechanism leading to their formation as well as their structure and function in acute myeloid leukemia (AML) remain mysterious. We combined a range of high-resolution genomic methods to investigate the architecture and expression pattern of amplicons involving chromosome band 8q24 in 23 cases of AML (AML-amp). This revealed that different MYC-dmin architectures can coexist within the same leukemic cell population, indicating a step-wise evolution rather than a single event origin, such as through chromothripsis. This was supported also by the analysis of the chromothripsis criteria, that poorly matched the model in our samples. Furthermore, we found that dmin could evolve toward ring chromosomes stabilized by neocentromeres. Surprisingly, amplified genes (mainly PVT1) frequently participated in fusion transcripts lacking a corresponding DNA template. We also detected a significant overexpression of the circular RNA of PVT1 (circPVT1) in AML-amp cases versus AML with a normal karyotype. Our results show that 8q24 amplicons in AML are surprisingly plastic DNA structures with an unexpected association to novel fusion transcripts and circular RNAs.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180303
[Lr] Last revision date:180303
[St] Status:Publisher
[do] DOI:10.1038/s41375-018-0033-0

  6 / 3523 MEDLINE  
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[PMID]: 29393095
[Au] Autor:Yamamoto K; Kawamoto S; Kurata K; Kitao A; Mizutani Y; Ichikawa H; Yakushijin K; Kajimoto K; Hayashi Y; Matsuoka H; Minami H
[Ad] Address:Division of Medical Oncology/Hematology, Department of Medicine, Kobe University Graduate School of Medicine, Kobe, Japan.
[Ti] Title:MYC Amplification in the Form of Ring Chromosomes 8 in Acute Myeloid Leukemia with t(11;16)(q13;p11.2).
[So] Source:Cytogenet Genome Res;153(3):131-137, 2017.
[Is] ISSN:1424-859X
[Cp] Country of publication:Switzerland
[La] Language:eng
[Ab] Abstract:Oncogene amplification is uncommon in acute myeloid leukemia (AML). Cytogenetically, it is primarily found as double minute chromosomes (dmin) or homogeneously staining regions (hsr). A 62-year-old woman was admitted to our hospital because of anemia and thrombocytopenia. Her bone marrow was hypercellular with 78.6% myeloperoxidase- positive blasts. Some had micronuclei. The patient was diagnosed with AML M2 and remains in complete remission (CR) after induction therapy. G-banding at diagnosis showed 51,XX,t(11;16)(q13;p11.2),+r1,+mar1×4. Spectral karyotyping confirmed t(11;16) and revealed that the ring and the marker chromosomes were derived from multiple copies of ring chromosome 8. Fluorescence in situ hybridization (FISH) with a MYC probe at 8q24 detected amplified MYC signals on 1 large and 4 small ring chromosomes 8. One MYC signal was deleted from one of the 2 chromosomes 8. FISH with a FUS probe at 16p11.2 showed monoallelic deletion of FUS. Immunohistochemistry demonstrated MYC protein overexpression at diagnosis and almost negative expression in CR. These results indicate that MYC amplification could occur in ring chromosomes without dmin. A cryptic MYC deletion suggests that an episome model could be applicable to MYC amplification in ring chromosomes as observed for dmin and hsr. Furthermore, considering 2 further reported cases, t(11;16)(q13;p11) may be a very rare but recurrent translocation in AML.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180228
[Lr] Last revision date:180228
[St] Status:In-Process
[do] DOI:10.1159/000486328

  7 / 3523 MEDLINE  
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[PMID]: 29486464
[Au] Autor:Danilova TV; Friebe B; Gill BS; Poland J; Jackson E
[Ad] Address:Wheat Genetics Resource Center, Department of Plant Pathology, Throckmorton Plant Sciences Center, Kansas State University, Manhattan, KS, USA.
[Ti] Title:Chromosome Rearrangements Caused by Double Monosomy in Wheat-Barley Group-7 Substitution Lines.
[So] Source:Cytogenet Genome Res;, 2018 Feb 28.
[Is] ISSN:1424-859X
[Cp] Country of publication:Switzerland
[La] Language:eng
[Ab] Abstract:Interspecific or introgressive hybridization is one of the driving forces in plant speciation, producing allopolyploids or diploids with rearranged genomes. The process of karyotype reshaping following homoploid interspecific hybridization has not been studied experimentally. Interspecific hybridization is widely used in plant breeding to increase genetic diversity and introgress new traits. Numerous introgression stocks were developed for hexaploid wheat Triticum aestivum L. (2n = 6x = 42, genome AABBDD). Double monosomic lines, containing one alien chromosome from the tertiary gene pool of wheat and one homoeologous wheat chromosome, represent a simplified model for studying chromosome rearrangements caused by interspecific hybridization. The pairing of a chromosome from the tertiary gene pool with a wheat homoeologue is restricted by the activity of the wheat Ph1 gene, thus, rearrangements caused by chromosome breakage followed by the fusion of the broken arms can be expected. We analyzed chromosome aberrations in 4 sets of lines that originated from double monosomics of barley (Hordeum vulgare L.) chromosome 7H and wheat group-7 chromosomes with dicentric or ring chromosomes. The dynamics of wheat-barley dicentric chromosomes during plant development was followed and an increased diversity of rearrangements was observed. Besides the targeted group-7 chromosomes, other wheat chromosomes were involved in rearrangements, as chromosomes broken in the centromeric region fused with other broken chromosomes. In some cells, multi-centric chromosomes were observed. The structure and dosage of the introgressed barley chromatin was changed. The transmission of the rearrangements to the progenies was analyzed. The observed aberrations emphasize the importance of cytogenetic screening in gene introgression projects.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180227
[Lr] Last revision date:180227
[St] Status:Publisher
[do] DOI:10.1159/000487183

  8 / 3523 MEDLINE  
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[PMID]: 28453390
[Au] Autor:Chavda AP; Ang K; Ivanov D
[Ad] Address:a Bioinformatics Institute, A*STAR , Singapore.
[Ti] Title:The torments of the cohesin ring.
[So] Source:Nucleus;8(3):261-267, 2017 May 04.
[Is] ISSN:1949-1042
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Cohesin is a ring-shaped protein complex which comprises the Smc1, Smc3 and Scc1 subunits. It topologically embraces chromosomal DNA to connect sister chromatids and stabilize chromatin loops. It is required for proper chromosomal segregation, DNA repair and transcriptional regulation. We have recently reported that cohesin rings can adopt a "collapsed" rod-like conformation which is driven by the interaction between the Smc1 and Smc3 coiled coil arms and is regulated by post-translational modifications. The "collapsed" conformation plays a role in cohesin ring assembly and its loading on the DNA. Here we speculate about the mechanism of cohesin's conformational transitions in relation to its loading on the DNA and draw parallels with other Smc-like complexes.
[Mh] MeSH terms primary: Cell Cycle Proteins/metabolism
Chromosomal Proteins, Non-Histone/metabolism
[Mh] MeSH terms secundary: Adenosine Triphosphate/metabolism
Animals
Cell Cycle Proteins/chemistry
Chromosomal Proteins, Non-Histone/chemistry
DNA/genetics
DNA/metabolism
Humans
Hydrolysis
Protein Conformation
Protein Processing, Post-Translational
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:0 (Cell Cycle Proteins); 0 (Chromosomal Proteins, Non-Histone); 0 (cohesins); 8L70Q75FXE (Adenosine Triphosphate); 9007-49-2 (DNA)
[Em] Entry month:1802
[Cu] Class update date: 180227
[Lr] Last revision date:180227
[Js] Journal subset:IM
[Da] Date of entry for processing:170429
[St] Status:MEDLINE
[do] DOI:10.1080/19491034.2017.1295200

  9 / 3523 MEDLINE  
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[PMID]: 29472722
[Au] Autor:Fontana MC; Marconi G; Feenstra JDM; Fonzi E; Papayannidis C; Ghelli Luserna di Rorá A; Padella A; Solli V; Franchini E; Ottaviani E; Ferrari A; Baldazzi C; Testoni N; Iacobucci I; Soverini S; Haferlach T; Guadagnuolo V; Semerad L; Doubek M; Steurer M; Racil Z; Paolini S; Manfrini M; Cavo M; Simonetti G; Kralovics R; Martinelli G
[Ad] Address:Institute of Hematology "L. and A. Seràgnoli", University of Bologna, Bologna, Italy. mariachiara.fontana4@unibo.it.
[Ti] Title:Chromothripsis in acute myeloid leukemia: biological features and impact on survival.
[So] Source:Leukemia;, 2018 Feb 23.
[Is] ISSN:1476-5551
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Chromothripsis is a one-step genome-shattering catastrophe resulting from disruption of one or few chromosomes in multiple fragments and consequent random rejoining and repair. This study defines incidence of chromothripsis in 395 newly diagnosed adult acute myeloid leukemia (AML) patients from three institutions, its impact on survival and its genomic background. SNP 6.0 or CytoscanHD Array (Affymetrix ) were performed on all samples. We detected chromothripsis with a custom algorithm in 26/395 patients. Patients harboring chromothripsis had higher age (p = 0.002), ELN high risk (HR) (p < 0.001), lower white blood cell (WBC) count (p = 0.040), TP53 loss, and/or mutations (p < 0.001) while FLT3 (p = 0.025), and NPM1 (p = 0.032) mutations were mutually exclusive with chromothripsis. Chromothripsis-positive patients showed a worse overall survival (OS) (p < 0.001) compared with HR patients (p = 0.011) and a poor prognosis in a COX-HR optimal regression model. Chromothripsis presented the hallmarks of chromosome instability [i.e., TP53 alteration, 5q deletion, higher mean of copy number alteration (CNA), complex karyotype, alterations in DNA repair, and cell cycle] and focal deletions on chromosomes 4, 7, 12, 16, and 17. CBA. FISH showed that chromothripsis is associated with marker, derivative, and ring chromosomes. In conclusion, chromothripsis frequently occurs in AML (6.6%) and influences patient prognosis and disease biology.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180223
[Lr] Last revision date:180223
[St] Status:Publisher
[do] DOI:10.1038/s41375-018-0035-y

  10 / 3523 MEDLINE  
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[PMID]: 29452641
[Au] Autor:Thattikota Y; Tollis S; Palou R; Vinet J; Tyers M; D'Amours D
[Ad] Address:Institute for Research in Immunology and Cancer, Université de Montréal, C.P. 6128, succursale Centre-ville, Montréal, QC H3C 3J7, Canada; Ottawa Institute of Systems Biology, Department of Cellular and Molecular Medicine, University of Ottawa, Roger Guindon Hall, 451 Smyth Road, Ottawa, ON K1H 8M5,
[Ti] Title:Cdc48/VCP Promotes Chromosome Morphogenesis by Releasing Condensin from Self-Entrapment in Chromatin.
[So] Source:Mol Cell;69(4):664-676.e5, 2018 Feb 15.
[Is] ISSN:1097-4164
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:The morphological transformation of amorphous chromatin into distinct chromosomes is a hallmark of mitosis. To achieve this, chromatin must be compacted and remodeled by a ring-shaped enzyme complex known as condensin. However, the mechanistic basis underpinning condensin's role in chromosome remodeling has remained elusive. Here we show that condensin has a strong tendency to trap itself in its own reaction product during chromatin compaction and yet is capable of interacting with chromatin in a highly dynamic manner in vivo. To resolve this apparent paradox, we identified specific chromatin remodelers and AAA-class ATPases that act in a coordinated manner to release condensin from chromatin entrapment. The Cdc48 segregase is the central linchpin of this regulatory mechanism and promotes ubiquitin-dependent cycling of condensin on mitotic chromatin as well as effective chromosome condensation. Collectively, our results show that condensin inhibition by its own reaction product is relieved by forceful enzyme extraction from chromatin.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180217
[Lr] Last revision date:180217
[St] Status:In-Data-Review


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