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  1. Article ; Online: ATRX/DAXX: Guarding the Genome against the Hazards of ALT

    Clatterbuck Soper, Sarah F. / Meltzer, Paul S.

    Genes (Basel). 2023 Mar. 24, v. 14, no. 4

    2023  

    Abstract: Proliferating cells must enact a telomere maintenance mechanism to ensure genomic stability. In a subset of tumors, telomeres are maintained not by telomerase, but through a homologous recombination-based mechanism termed Alternative Lengthening of ... ...

    Abstract Proliferating cells must enact a telomere maintenance mechanism to ensure genomic stability. In a subset of tumors, telomeres are maintained not by telomerase, but through a homologous recombination-based mechanism termed Alternative Lengthening of Telomeres or ALT. The ALT process is linked to mutations in the ATRX/DAXX/H3.3 histone chaperone complex. This complex is responsible for depositing non-replicative histone variant H3.3 at pericentric and telomeric heterochromatin but has also been found to have roles in ameliorating replication in repeat sequences and in promoting DNA repair. In this review, we will discuss ways in which ATRX/DAXX helps to protect the genome, and how loss of this complex allows ALT to take hold.
    Keywords DNA repair ; genome ; genomics ; heterochromatin ; histones ; telomerase ; telomeres
    Language English
    Dates of publication 2023-0324
    Publishing place Multidisciplinary Digital Publishing Institute
    Document type Article ; Online
    ZDB-ID 2527218-4
    ISSN 2073-4425
    ISSN 2073-4425
    DOI 10.3390/genes14040790
    Database NAL-Catalogue (AGRICOLA)

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  2. Article ; Online: ATRX/DAXX: Guarding the Genome against the Hazards of ALT.

    Clatterbuck Soper, Sarah F / Meltzer, Paul S

    Genes

    2023  Volume 14, Issue 4

    Abstract: Proliferating cells must enact a telomere maintenance mechanism to ensure genomic stability. In a subset of tumors, telomeres are maintained not by telomerase, but through a homologous recombination-based mechanism termed Alternative Lengthening of ... ...

    Abstract Proliferating cells must enact a telomere maintenance mechanism to ensure genomic stability. In a subset of tumors, telomeres are maintained not by telomerase, but through a homologous recombination-based mechanism termed Alternative Lengthening of Telomeres or ALT. The ALT process is linked to mutations in the ATRX/DAXX/H3.3 histone chaperone complex. This complex is responsible for depositing non-replicative histone variant H3.3 at pericentric and telomeric heterochromatin but has also been found to have roles in ameliorating replication in repeat sequences and in promoting DNA repair. In this review, we will discuss ways in which ATRX/DAXX helps to protect the genome, and how loss of this complex allows ALT to take hold.
    MeSH term(s) X-linked Nuclear Protein/genetics ; Telomere Homeostasis/genetics ; Molecular Chaperones/genetics ; Histones/genetics ; Telomerase/genetics ; Telomerase/metabolism
    Chemical Substances X-linked Nuclear Protein (EC 3.6.4.12) ; Molecular Chaperones ; Histones ; Telomerase (EC 2.7.7.49)
    Language English
    Publishing date 2023-03-24
    Publishing country Switzerland
    Document type Journal Article ; Review ; Research Support, N.I.H., Intramural
    ZDB-ID 2527218-4
    ISSN 2073-4425 ; 2073-4425
    ISSN (online) 2073-4425
    ISSN 2073-4425
    DOI 10.3390/genes14040790
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: FUS inclusions disrupt RNA localization by sequestering kinesin-1 and inhibiting microtubule detyrosination.

    Yasuda, Kyota / Clatterbuck-Soper, Sarah F / Jackrel, Meredith E / Shorter, James / Mili, Stavroula

    The Journal of cell biology

    2017  Volume 216, Issue 4, Page(s) 1015–1034

    Abstract: Cytoplasmic inclusions of the RNA-binding protein fused in sarcoma (FUS) represent one type of membraneless ribonucleoprotein compartment. Formation of FUS inclusions is promoted by amyotrophic lateral sclerosis (ALS)-linked mutations, but the cellular ... ...

    Abstract Cytoplasmic inclusions of the RNA-binding protein fused in sarcoma (FUS) represent one type of membraneless ribonucleoprotein compartment. Formation of FUS inclusions is promoted by amyotrophic lateral sclerosis (ALS)-linked mutations, but the cellular functions affected upon inclusion formation are poorly defined. In this study, we find that FUS inclusions lead to the mislocalization of specific RNAs from fibroblast cell protrusions and neuronal axons. This is mediated by recruitment of kinesin-1 mRNA and protein within FUS inclusions, leading to a loss of detyrosinated glutamate (Glu)-microtubules (MTs; Glu-MTs) and an inability to support the localization of RNAs at protrusions. Importantly, dissolution of FUS inclusions using engineered Hsp104 disaggregases, or overexpression of kinesin-1, reverses these effects. We further provide evidence that kinesin-1 affects MT detyrosination not through changes in MT stability, but rather through targeting the tubulin carboxypeptidase enzyme onto specific MTs. Interestingly, other pathological inclusions lead to similar outcomes, but through apparently distinct mechanisms. These results reveal a novel kinesin-dependent mechanism controlling the MT cytoskeleton and identify loss of Glu-MTs and RNA mislocalization as common outcomes of ALS pathogenic mutations.
    MeSH term(s) Amyotrophic Lateral Sclerosis/metabolism ; Amyotrophic Lateral Sclerosis/pathology ; Animals ; Cell Line ; Cytoplasm/metabolism ; Cytoplasm/physiology ; Glutamic Acid/metabolism ; Inclusion Bodies/metabolism ; Inclusion Bodies/physiology ; Kinesin/metabolism ; Mice ; Microtubules/metabolism ; Microtubules/physiology ; Mutation/physiology ; NIH 3T3 Cells ; Protein Transport/physiology ; RNA/metabolism ; RNA, Messenger/metabolism ; RNA-Binding Protein FUS/metabolism ; RNA-Binding Proteins/metabolism ; Sarcoma/metabolism ; Sarcoma/pathology ; Tubulin/metabolism ; Tubulin Modulators/metabolism ; Tyrosine/metabolism
    Chemical Substances RNA, Messenger ; RNA-Binding Protein FUS ; RNA-Binding Proteins ; Tubulin ; Tubulin Modulators ; Glutamic Acid (3KX376GY7L) ; Tyrosine (42HK56048U) ; RNA (63231-63-0) ; Kinesin (EC 3.6.4.4)
    Language English
    Publishing date 2017-04-03
    Publishing country United States
    Document type Journal Article
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.201608022
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ub I Zs.190: Show issues Location:
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    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  4. Article ; Online: Rapid and reversible suppression of ALT by DAXX in osteosarcoma cells.

    Yost, Kathryn E / Clatterbuck Soper, Sarah F / Walker, Robert L / Pineda, Marbin A / Zhu, Yuelin J / Ester, Corbin D / Showman, Soyeon / Roschke, Anna V / Waterfall, Joshua J / Meltzer, Paul S

    Scientific reports

    2019  Volume 9, Issue 1, Page(s) 4544

    Abstract: Many tumors maintain chromosome-ends through a telomerase-independent, DNA-templated mechanism called alternative lengthening of telomeres (ALT). While ALT occurs in only a subset of tumors, it is strongly associated with mutations in the genes ATRX and ... ...

    Abstract Many tumors maintain chromosome-ends through a telomerase-independent, DNA-templated mechanism called alternative lengthening of telomeres (ALT). While ALT occurs in only a subset of tumors, it is strongly associated with mutations in the genes ATRX and DAXX, which encode components of an H3.3 histone chaperone complex. The role of ATRX and DAXX mutations in potentiating the mechanism of ALT remains incompletely understood. Here we characterize an osteosarcoma cell line, G292, with wild-type ATRX but a unique chromosome translocation resulting in loss of DAXX function. While ATRX and DAXX form a complex in G292, this complex fails to localize to nuclear PML bodies. We demonstrate that introduction of wild type DAXX suppresses the ALT phenotype and restores the localization of ATRX/DAXX to PML bodies. Using an inducible system, we show that ALT-associated PML bodies are disrupted rapidly following DAXX induction and that ALT is again restored following withdrawal of DAXX.
    MeSH term(s) Bone Neoplasms/genetics ; Bone Neoplasms/pathology ; Co-Repressor Proteins/genetics ; Humans ; Molecular Chaperones/genetics ; Mutation ; Osteosarcoma/genetics ; Osteosarcoma/pathology ; Phenotype ; Telomerase/genetics ; Telomerase/metabolism ; Telomere Homeostasis ; Tumor Cells, Cultured
    Chemical Substances Co-Repressor Proteins ; DAXX protein, human ; Molecular Chaperones ; TERT protein, human (EC 2.7.7.49) ; Telomerase (EC 2.7.7.49)
    Language English
    Publishing date 2019-03-14
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Intramural
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-019-41058-8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: In vivo X-ray footprinting of pre-30S ribosomes reveals chaperone-dependent remodeling of late assembly intermediates.

    Clatterbuck Soper, Sarah F / Dator, Romel P / Limbach, Patrick A / Woodson, Sarah A

    Molecular cell

    2013  Volume 52, Issue 4, Page(s) 506–516

    Abstract: Assembly of 30S ribosomal subunits from their protein and RNA components requires extensive refolding of the 16S rRNA and is assisted by 10-20 assembly factors in bacteria. We probed the structures of 30S assembly intermediates in E. coli cells, using a ... ...

    Abstract Assembly of 30S ribosomal subunits from their protein and RNA components requires extensive refolding of the 16S rRNA and is assisted by 10-20 assembly factors in bacteria. We probed the structures of 30S assembly intermediates in E. coli cells, using a synchrotron X-ray beam to generate hydroxyl radical in the cytoplasm. Widespread differences between mature and pre-30S complexes in the absence of assembly factors RbfA and RimM revealed global reorganization of RNA-protein interactions prior to maturation of the 16S rRNA and showed how RimM reduces misfolding of the 16S 3' domain during transcription in vivo. Quantitative (14)N/(15)N mass spectrometry of affinity-purified pre-30S complexes confirmed the absence of tertiary assembly proteins and showed that N-terminal acetylation of proteins S18 and S5 correlates with correct folding of the platform and central pseudoknot. Our results indicate that cellular factors delay specific RNA folding steps to ensure the quality of assembly.
    MeSH term(s) Acetylation ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Gene Deletion ; Inverted Repeat Sequences ; Models, Molecular ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Nucleic Acid Conformation ; Protein Multimerization ; Protein Processing, Post-Translational ; RNA Cleavage/radiation effects ; RNA Folding ; RNA, Ribosomal, 16S/chemistry ; RNA, Ribosomal, 16S/metabolism ; Ribosomal Proteins/genetics ; Ribosomal Proteins/metabolism ; Ribosome Subunits, Small, Bacterial/metabolism ; Transcription, Genetic
    Chemical Substances Escherichia coli Proteins ; Molecular Chaperones ; RNA, Ribosomal, 16S ; RbfA protein, E coli ; Ribosomal Proteins ; RimM protein, E coli
    Language English
    Publishing date 2013-10-24
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2013.09.020
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5055: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  6. Article: In Vivo X-Ray Footprinting of Pre-30S Ribosomes Reveals Chaperone-Dependent Remodeling of Late Assembly Intermediates

    Clatterbuck Soper, Sarah F. / Dator, Romel P. / Limbach, Patrick A. / Woodson, Sarah A.

    Molecular cell

    Volume v. 52,, Issue no. 4

    Abstract: Assembly of 30S ribosomal subunits from their protein and RNA components requires extensive refolding of the 16S rRNA and is assisted by 10–20 assembly factors in bacteria. We probed the structures of 30S assembly intermediates in E. coli cells, using a ... ...

    Abstract Assembly of 30S ribosomal subunits from their protein and RNA components requires extensive refolding of the 16S rRNA and is assisted by 10–20 assembly factors in bacteria. We probed the structures of 30S assembly intermediates in E. coli cells, using a synchrotron X-ray beam to generate hydroxyl radical in the cytoplasm. Widespread differences between mature and pre-30S complexes in the absence of assembly factors RbfA and RimM revealed global reorganization of RNA-protein interactions prior to maturation of the 16S rRNA and showed how RimM reduces misfolding of the 16S 3′ domain during transcription in vivo. Quantitative ¹⁴N/¹⁵N mass spectrometry of affinity-purified pre-30S complexes confirmed the absence of tertiary assembly proteins and showed that N-terminal acetylation of proteins S18 and S5 correlates with correct folding of the platform and central pseudoknot. Our results indicate that cellular factors delay specific RNA folding steps to ensure the quality of assembly.
    Keywords hydroxyl radicals ; ribosomal RNA ; RNA folding ; ribosomes ; acetylation ; ribosomal proteins ; mass spectrometry ; bacteria ; Escherichia coli ; proteins ; protein subunits ; X-radiation
    Language English
    Document type Article
    ISSN 1097-2765
    Database AGRIS - International Information System for the Agricultural Sciences and Technology

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