LIVIVO - Search results -

Search results

Result 1 - 10 of total 101

Search options

Article ; Online: The anatomy of a nucleus: As revealed by chromosome painting.

Slaughter, Brian D / Hawley, R Scott

2018 Volume 14, Issue 7, Page(s) e1007445

MeSH term(s)	Adenosine Triphosphatases ; Animals ; Chromosome Painting ; Chromosomes ; DNA-Binding Proteins ; Drosophila ; Interphase ; Karyotyping ; Multiprotein Complexes
Chemical Substances	DNA-Binding Proteins ; Multiprotein Complexes ; condensin complexes ; Adenosine Triphosphatases (EC 3.6.1.-)
Language	English
Publishing date	2018-07-12
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	2186725-2
ISSN	1553-7404 ; 1553-7390
ISSN (online)	1553-7404
ISSN	1553-7390
DOI	10.1371/journal.pgen.1007445
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Article ; Online: Multiple reorganizations of the lateral elements of the synaptonemal complex facilitate homolog segregation in Bombyx mori oocytes.

Xiang, Youbin / Tsuchiya, Dai / Yu, Zulin / Zhao, Xia / McKinney, Sean / Unruh, Jay / Slaughter, Brian / Lake, Cathleen M / Hawley, R Scott

Current biology : CB

2024 Volume 34, Issue 2, Page(s) 352–360.e4

Abstract: Although Lepidopteran females build a synaptonemal complex (SC) in pachytene, homologs do not crossover, necessitating an alternative method of homolog conjunction. In Bombyx mori oocytes, the SC breaks down at the end of pachytene, and homolog ... ...

Abstract	Although Lepidopteran females build a synaptonemal complex (SC) in pachytene, homologs do not crossover, necessitating an alternative method of homolog conjunction. In Bombyx mori oocytes, the SC breaks down at the end of pachytene, and homolog associations are maintained by a large oocyte-specific structure, which we call the bivalent bridge (BB), connecting paired homologs. The BB is derived from at least some components of the SC lateral elements (LEs). It contains the HORMAD protein HOP1 and the LE protein SYCP2 and is formed by the fusion of the two LE derivatives. As diplotene progresses, the BB increases in width and acquires a layered structure with a thick band of HOP1 separating two layers of SYCP2. The HOP1 interacting protein, PCH2, joins the BB in mid-diplotene, and by late-diplotene, it lies in the middle of the HOP1 filament. This structure is maintained through metaphase I. SYCP2 and PCH2 are lost at anaphase I, and the BB no longer connects the separating homologs. However, a key component of the BB, HOP1, remains at the metaphase I plate. These changes in organization of the BB occur simultaneously with the movement of the kinetochore protein, DSN1, from within the BB at mid-diplotene to the edge of the homologs facing the poles by metaphase I. We view these data in context of models in which SC components and regulators can be repurposed to achieve different functions, a fascinating example of evolution achieving homolog conjunction in an alternative way with recycling of SC proteins.
MeSH term(s)	Animals ; Female ; Synaptonemal Complex ; Bombyx ; Meiosis ; Oocytes/metabolism ; Metaphase
Language	English
Publishing date	2024-01-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2023.12.018
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 3208: 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)

Order via subito

Details ▾

Article ; Online: Super-resolution Microscopy-based Bimolecular Fluorescence Complementation to Study Protein Complex Assembly and Co-localization.

Chen, Jingjing / Yu, Zulin / Unruh, Jay R / Slaughter, Brian D / Jaspersen, Sue L

Bio-protocol

2020 Volume 10, Issue 4, Page(s) e3524

Abstract: Numerous experimental approaches exist to study interactions between two subunits of a large macromolecular complex. However, most methods do not provide spatial and temporal information about binding, which are critical for dissecting the mechanism of ... ...

Abstract	Numerous experimental approaches exist to study interactions between two subunits of a large macromolecular complex. However, most methods do not provide spatial and temporal information about binding, which are critical for dissecting the mechanism of assembly of nanosized complexes
Language	English
Publishing date	2020-02-20
Publishing country	United States
Document type	Journal Article
ZDB-ID	2833269-6
ISSN	2331-8325 ; 2331-8325
ISSN (online)	2331-8325
ISSN	2331-8325
DOI	10.21769/BioProtoc.3524
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Functional Analysis of the Yeast LINC Complex Using Fluctuation Spectroscopy and Super-Resolution Imaging.

Unruh, Jay R / Slaughter, Brian D / Jaspersen, Sue L

Methods in molecular biology (Clifton, N.J.)

2018 Volume 1840, Page(s) 137–161

Abstract: The Saccharomyces cerevisiae and Schizosaccharomyces pombe genomes encode a single SUN domain-containing protein, Mps3 and Sad1, respectively. Both localize to the yeast centrosome (known as the spindle pole body, SPB) and are essential for bipolar ... ...

Abstract	The Saccharomyces cerevisiae and Schizosaccharomyces pombe genomes encode a single SUN domain-containing protein, Mps3 and Sad1, respectively. Both localize to the yeast centrosome (known as the spindle pole body, SPB) and are essential for bipolar spindle formation. In addition, Mps3 and Sad1 play roles in chromosome organization in both mitotic and meiotic cells that are independent of their SPB function. To dissect the function of Mps3 at the nuclear envelope (NE) and SPB, we employed cell imaging methods such as scanning fluorescence cross-correlation spectroscopy (SFCCS) and single particle averaging with structured illumination microscopy (SPA-SIM) to determine the strength, nature, and location of protein-protein interactions in vivo. We describe how these same techniques can also be used in fission yeast to analyze Sad1, providing evidence of their applicability to other NE proteins and systems.
MeSH term(s)	Cytoskeleton/metabolism ; Fluorescent Antibody Technique ; Fungal Proteins/metabolism ; Gene Expression ; Genes, Reporter ; Nuclear Envelope/metabolism ; Nuclear Proteins/metabolism ; Saccharomyces cerevisiae/metabolism ; Schizosaccharomyces/metabolism ; Spectrum Analysis/methods
Chemical Substances	Fungal Proteins ; Nuclear Proteins
Language	English
Publishing date	2018-09-07
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-8691-0_12
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Lola-I is a promoter pioneer factor that establishes de novo Pol II pausing during development.

Ramalingam, Vivekanandan / Yu, Xinyang / Slaughter, Brian D / Unruh, Jay R / Brennan, Kaelan J / Onyshchenko, Anastasiia / Lange, Jeffrey J / Natarajan, Malini / Buck, Michael / Zeitlinger, Julia

Nature communications

2023 Volume 14, Issue 1, Page(s) 5862

Abstract: While the accessibility of enhancers is dynamically regulated during development, promoters tend to be constitutively accessible and poised for activation by paused Pol II. By studying Lola-I, a Drosophila zinc finger transcription factor, we show here ... ...

Abstract	While the accessibility of enhancers is dynamically regulated during development, promoters tend to be constitutively accessible and poised for activation by paused Pol II. By studying Lola-I, a Drosophila zinc finger transcription factor, we show here that the promoter state can also be subject to developmental regulation independently of gene activation. Lola-I is ubiquitously expressed at the end of embryogenesis and causes its target promoters to become accessible and acquire paused Pol II throughout the embryo. This promoter transition is required but not sufficient for tissue-specific target gene activation. Lola-I mediates this function by depleting promoter nucleosomes, similar to the action of pioneer factors at enhancers. These results uncover a level of regulation for promoters that is normally found at enhancers and reveal a mechanism for the de novo establishment of paused Pol II at promoters.
MeSH term(s)	Animals ; Promoter Regions, Genetic/genetics ; Drosophila/genetics ; Embryo, Mammalian ; Embryonic Development ; Nucleosomes/genetics ; RNA Polymerase II/genetics
Chemical Substances	Nucleosomes ; RNA Polymerase II (EC 2.7.7.-)
Language	English
Publishing date	2023-09-21
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-41408-1
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: Serial Capture Affinity Purification and Integrated Structural Modeling of the H3K4me3 Binding and DNA Damage Related WDR76:SPIN1 Complex.

Liu, Xingyu / Zhang, Ying / Wen, Zhihui / Hao, Yan / Banks, Charles A S / Lange, Jeffrey J / Cesare, Joseph / Bhattacharya, Saikat / Slaughter, Brian D / Unruh, Jay R / Florens, Laurence / Workman, Jerry L / Washburn, Michael P

bioRxiv : the preprint server for biology

2023

Abstract: WDR76 is a multifunctional protein involved in many cellular functions. With a diverse and complicated protein interaction network, dissecting the structure and function of specific WDR76 complexes is needed. We previously demonstrated the ability of the ...

Abstract	WDR76 is a multifunctional protein involved in many cellular functions. With a diverse and complicated protein interaction network, dissecting the structure and function of specific WDR76 complexes is needed. We previously demonstrated the ability of the Serial Capture Affinity Purification (SCAP) method to isolate specific complexes by introducing two proteins of interest as baits at the same time. Here, we applied SCAP to dissect a subpopulation of WDR76 in complex with SPIN1, a histone marker reader that specifically recognizes trimethylated histone H3 lysine4 (H3K4me3). In contrast to the SCAP analysis of the SPIN1:SPINDOC complex, H3K4me3 was copurified with the WDR76:SPIN1 complex. In combination with crosslinking mass spectrometry, we built an integrated structural model of the complex which revealed that SPIN1 recognized the H3K4me3 epigenetic mark while interacting with WDR76. Lastly, interaction network analysis of copurifying proteins revealed the potential role of the WDR76:SPIN1 complex in the DNA damage response. Teaser: In contrast to the SPINDOC/SPIN1 complex, analyses reveal that the WDR76/SPIN1 complex interacts with core histones and is involved in DNA damage.
Language	English
Publishing date	2023-02-03
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.01.31.526478
Database	MEDical Literature Analysis and Retrieval System OnLINE

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾

Article ; Online: Shared retinoic acid responsive enhancers coordinately regulate nascent transcription of Hoxb coding and non-coding RNAs in the developing mouse neural tube.

Afzal, Zainab / Lange, Jeffrey J / Nolte, Christof / McKinney, Sean / Wood, Christopher / Paulson, Ariel / De Kumar, Bony / Unruh, Jay / Slaughter, Brian D / Krumlauf, Robb

Development (Cambridge, England)

2023 Volume 150, Issue 10

Abstract: Signaling pathways regulate the patterns of Hox gene expression that underlie their functions in the specification of axial identity. Little is known about the properties of cis-regulatory elements and underlying transcriptional mechanisms that integrate ...

Abstract	Signaling pathways regulate the patterns of Hox gene expression that underlie their functions in the specification of axial identity. Little is known about the properties of cis-regulatory elements and underlying transcriptional mechanisms that integrate graded signaling inputs to coordinately control Hox expression. Here, we optimized a single molecule fluorescent in situ hybridization (smFISH) technique with probes spanning introns to evaluate how three shared retinoic acid response element (RARE)-dependent enhancers in the Hoxb cluster regulate patterns of nascent transcription in vivo at the level of single cells in wild-type and mutant embryos. We predominately detect nascent transcription of only a single Hoxb gene in each cell, with no evidence for simultaneous co-transcriptional coupling of all or specific subsets of genes. Single and/or compound RARE mutations indicate that each enhancer differentially impacts global and local patterns of nascent transcription, suggesting that selectivity and competitive interactions between these enhancers is important to robustly maintain the proper levels and patterns of nascent Hoxb transcription. This implies that rapid and dynamic regulatory interactions potentiate transcription of genes through combined inputs from these enhancers in coordinating the retinoic acid response.
MeSH term(s)	Mice ; Animals ; Tretinoin/metabolism ; Homeodomain Proteins/metabolism ; Mice, Transgenic ; Neural Tube/metabolism ; In Situ Hybridization, Fluorescence ; Enhancer Elements, Genetic
Chemical Substances	Tretinoin (5688UTC01R) ; Homeodomain Proteins
Language	English
Publishing date	2023-05-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	90607-4
ISSN	1477-9129 ; 0950-1991
ISSN (online)	1477-9129
ISSN	0950-1991
DOI	10.1242/dev.201259
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Ub I Zs.183: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Zs.MG 91: Show issues

Order via subito

Details ▾

Article ; Online: Lola-I is a promoter pioneer factor that establishes de novo Pol II pausing during development

Vivekanandan Ramalingam / Xinyang Yu / Brian D. Slaughter / Jay R. Unruh / Kaelan J. Brennan / Anastasiia Onyshchenko / Jeffrey J. Lange / Malini Natarajan / Michael Buck / Julia Zeitlinger

Nature Communications, Vol 14, Iss 1, Pp 1-

2023 Volume 14

Abstract: Abstract While the accessibility of enhancers is dynamically regulated during development, promoters tend to be constitutively accessible and poised for activation by paused Pol II. By studying Lola-I, a Drosophila zinc finger transcription factor, we ... ...

Abstract	Abstract While the accessibility of enhancers is dynamically regulated during development, promoters tend to be constitutively accessible and poised for activation by paused Pol II. By studying Lola-I, a Drosophila zinc finger transcription factor, we show here that the promoter state can also be subject to developmental regulation independently of gene activation. Lola-I is ubiquitously expressed at the end of embryogenesis and causes its target promoters to become accessible and acquire paused Pol II throughout the embryo. This promoter transition is required but not sufficient for tissue-specific target gene activation. Lola-I mediates this function by depleting promoter nucleosomes, similar to the action of pioneer factors at enhancers. These results uncover a level of regulation for promoters that is normally found at enhancers and reveal a mechanism for the de novo establishment of paused Pol II at promoters.
Keywords	Science ; Q
Language	English
Publishing date	2023-09-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Condensin II is anchored by TFIIIC and H3K4me3 in the mammalian genome and supports the expression of active dense gene clusters.

Yuen, Kobe C / Slaughter, Brian D / Gerton, Jennifer L

Science advances

2017 Volume 3, Issue 6, Page(s) e1700191

Abstract: Structural maintenance of chromosome complexes, such as cohesin, have been implicated in a wide variety of chromatin-dependent functions such as genome organization, replication, and gene expression. How these complexes find their sites of association ... ...

Abstract	Structural maintenance of chromosome complexes, such as cohesin, have been implicated in a wide variety of chromatin-dependent functions such as genome organization, replication, and gene expression. How these complexes find their sites of association and affect local chromosomal processes is not well understood. We report that condensin II, a complex distinct from cohesin, physically interacts with TFIIIC, and they both colocalize at active gene promoters in the mouse and human genomes, facilitated by interaction between NCAPD3 and the epigenetic mark H3K4me3. Condensin II is important for maintaining high levels of expression of the histone gene clusters as well as the interaction between these clusters in the mouse genome. Our findings suggest that condensin II is anchored to the mammalian genome by a combination of H3K4me3 and the sequence-specific binding of TFIIIC, and that condensin supports the expression of active gene-dense regions found at the boundaries of topological domains. Together, our results support a working model in which condensin II contributes to topological domain boundary-associated gene activity in the mammalian genome.
MeSH term(s)	Adenosine Triphosphatases/genetics ; Animals ; Chromatin Immunoprecipitation ; Chromosome Mapping ; DNA-Binding Proteins/genetics ; Epistasis, Genetic ; Gene Expression Regulation ; Genetic Linkage ; Genome ; High-Throughput Nucleotide Sequencing ; Histones/genetics ; Humans ; Mice ; Multigene Family ; Multiprotein Complexes/genetics ; Transcription Factors, TFIII/genetics
Chemical Substances	DNA-Binding Proteins ; Histones ; Multiprotein Complexes ; Transcription Factors, TFIII ; condensin complexes ; transcription factor TFIIIC ; Adenosine Triphosphatases (EC 3.6.1.-)
Language	English
Publishing date	2017-06-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.1700191
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: A role for the Cockayne Syndrome B (CSB)-Elongin ubiquitin ligase complex in signal-dependent RNA polymerase II transcription.

Weems, Juston C / Slaughter, Brian D / Unruh, Jay R / Weaver, Kyle J / Miller, Brandon D / Delventhal, Kym M / Conaway, Joan W / Conaway, Ronald C

The Journal of biological chemistry

2021 Volume 297, Issue 1, Page(s) 100862

Abstract: The Elongin complex was originally identified as an RNA polymerase II (RNAPII) elongation factor and subsequently as the substrate recognition component of a Cullin-RING E3 ubiquitin ligase. More recent evidence indicates that the Elongin ubiquitin ... ...

Abstract	The Elongin complex was originally identified as an RNA polymerase II (RNAPII) elongation factor and subsequently as the substrate recognition component of a Cullin-RING E3 ubiquitin ligase. More recent evidence indicates that the Elongin ubiquitin ligase assembles with the Cockayne syndrome B helicase (CSB) in response to DNA damage and can target stalled polymerases for ubiquitylation and removal from the genome. In this report, we present evidence that the CSB-Elongin ubiquitin ligase pathway has roles beyond the DNA damage response in the activation of RNAPII-mediated transcription. We observed that assembly of the CSB-Elongin ubiquitin ligase is induced not just by DNA damage, but also by a variety of signals that activate RNAPII-mediated transcription, including endoplasmic reticulum (ER) stress, amino acid starvation, retinoic acid, glucocorticoids, and doxycycline treatment of cells carrying several copies of a doxycycline-inducible reporter. Using glucocorticoid receptor (GR)-regulated genes as a model, we showed that glucocorticoid-induced transcription is accompanied by rapid recruitment of CSB and the Elongin ubiquitin ligase to target genes in a step that depends upon the presence of transcribing RNAPII on those genes. Consistent with the idea that the CSB-Elongin pathway plays a direct role in GR-regulated transcription, mouse cells lacking the Elongin subunit Elongin A exhibit delays in both RNAPII accumulation on and dismissal from target genes following glucocorticoid addition and withdrawal, respectively. Taken together, our findings bring to light a new role for the CSB-Elongin pathway in RNAPII-mediated transcription.
MeSH term(s)	Animals ; Cockayne Syndrome/enzymology ; Cockayne Syndrome/genetics ; DNA Helicases/chemistry ; DNA Helicases/genetics ; DNA Helicases/ultrastructure ; DNA Repair/genetics ; DNA Repair Enzymes/chemistry ; DNA Repair Enzymes/genetics ; DNA Repair Enzymes/ultrastructure ; Elongin/chemistry ; Elongin/genetics ; Elongin/ultrastructure ; Humans ; Mice ; Multiprotein Complexes/chemistry ; Multiprotein Complexes/genetics ; Multiprotein Complexes/ultrastructure ; Poly-ADP-Ribose Binding Proteins/chemistry ; Poly-ADP-Ribose Binding Proteins/genetics ; Poly-ADP-Ribose Binding Proteins/ultrastructure ; RNA Polymerase II/chemistry ; RNA Polymerase II/genetics ; Receptors, Glucocorticoid/chemistry ; Receptors, Glucocorticoid/genetics ; Ubiquitin/chemistry ; Ubiquitin/genetics ; Ubiquitin-Protein Ligases/chemistry ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/ultrastructure ; Ubiquitination/genetics
Chemical Substances	Elongin ; Multiprotein Complexes ; Poly-ADP-Ribose Binding Proteins ; Receptors, Glucocorticoid ; Ubiquitin ; CULL-RING ligase, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; RNA Polymerase II (EC 2.7.7.-) ; DNA Helicases (EC 3.6.4.-) ; ERCC6 protein, human (EC 3.6.4.12) ; DNA Repair Enzymes (EC 6.5.1.-)
Language	English
Publishing date	2021-06-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2021.100862
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.108: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

To top

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito