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Article ; Online: 1,6-Hexanediol Is Inducing Homologous Recombination by Releasing BLM from Assemblysomes in

Gombás, Bence György / Villányi, Zoltán

International journal of molecular sciences

2024 Volume 25, Issue 3

Abstract: We recently demonstrated that 1,6-hexanediol inhibits the formation of assemblysomes. These membraneless cell organelles have important roles in co-translational protein complex assembly and also store halfway translated DNA damage response proteins for ... ...

Abstract	We recently demonstrated that 1,6-hexanediol inhibits the formation of assemblysomes. These membraneless cell organelles have important roles in co-translational protein complex assembly and also store halfway translated DNA damage response proteins for a timely stress response. Recognizing the therapeutic potential of 1,6-hexanediol in dismantling assemblysomes likely to be involved in chemo- or radiotherapy resistance of tumor cells, we initiated an investigation into the properties of 1,6-hexanediol. Our particular interest was to determine if this compound induces DNA double-strand breaks by releasing the BLM helicase. Its yeast ortholog Sgs1 was confirmed to be a component of assemblysomes. The BLM helicase induces DNA damage when overexpressed due to the DNA double-strand breaks it generates during its normal function to repair DNA damage sites. It is evident that storing Sgs1 helicase in assemblysomes is crucial to express the full-length functional protein only in the event of DNA damage. Alternatively, if we dissolve assemblysomes using 1,6-hexanediol, ribosome-nascent chain complexes might become targets of ribosome quality control. We explored these possibilities and found, through the Drosophila wing-spot test assay, that 1,6-hexanediol induces DNA double-strand breaks. Lethality connected to recombination events following 1,6-hexanediol treatment can be mitigated by inducing DNA double-strand breaks with X-ray. Additionally, we confirmed that SMC5 recruits DmBLM to DNA damage sites, as knocking it down abolishes the rescue effect of DNA double-strand breaks on 1,6-hexanediol-induced lethality in
MeSH term(s)	Animals ; DNA/metabolism ; DNA Helicases/metabolism ; DNA Repair ; Drosophila/genetics ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Glycols ; Homologous Recombination ; RecQ Helicases/genetics ; RecQ Helicases/metabolism
Chemical Substances	DNA (9007-49-2) ; DNA Helicases (EC 3.6.4.-) ; Drosophila Proteins ; Glycols ; hexamethylene glycol (ZIA319275I) ; RecQ Helicases (EC 3.6.4.12) ; blm protein, Drosophila (EC 3.6.4.12)
Language	English
Publishing date	2024-01-28
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms25031611
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Article ; Online: Stress-Induced Changes in Nucleocytoplasmic Localization of Crucial Factors in Gene Expression Regulation.

Khamit, Ali / Chakraborty, Payal / Zahorán, Szabolcs / Villányi, Zoltán / Orvos, Hajnalka / Hermesz, Edit

International journal of molecular sciences

2024 Volume 25, Issue 7

Abstract: This study investigates the toxic effect of harmful materials, unfiltered by the placenta, on neonatal umbilical cord (UC) vessels, focusing on stress-induced adaptations in transcriptional and translational processes. It aims to analyze changes in ... ...

Abstract	This study investigates the toxic effect of harmful materials, unfiltered by the placenta, on neonatal umbilical cord (UC) vessels, focusing on stress-induced adaptations in transcriptional and translational processes. It aims to analyze changes in pathways related to mRNA condensate formation, transcriptional regulation, and DNA damage response under maternal smoking-induced stress. UC vessels from neonates born to smoking (Sm) and nonsmoking mothers (Ctr) were examined. Immunofluorescence staining and confocal microscopy assessed the localization of key markers, including Transcription Complex Subunit 1 (CNOT1) and the largest subunit of RNA polymerase II enzyme (RPB1). Additionally, markers of DNA damage response, such as Poly(ADP-ribose) polymerase-1, were evaluated. In Sm samples, dissolution of CNOT1 granules in UC vessels was observed, potentially aiding stalled translation and enhancing transcription via RPB1 assembly and translocation. Control vessels showed predominant cytoplasmic RPB1 localization. Despite adaptive responses, Sm endothelial cells exhibited significant damage, indicated by markers like Poly(ADP-ribose) polymerase-1. Ex vivo metal treatment on control vessels mirrored Sm sample alterations, emphasizing marker roles in cell survival under toxic exposure. Maternal smoking induces specific molecular adaptations in UC vessels, affecting mRNA condensate formation, transcriptional regulation, and DNA damage response pathways. Understanding these intricate molecular mechanisms could inform interventions to improve neonatal health outcomes and mitigate adverse effects of toxic exposure during pregnancy.
MeSH term(s)	Infant, Newborn ; Humans ; Female ; Pregnancy ; Endothelial Cells ; Gene Expression Regulation ; Transcription, Genetic ; Cone-Rod Dystrophies ; Poly(ADP-ribose) Polymerases ; RNA, Messenger/genetics ; Transcription Factors
Chemical Substances	Poly(ADP-ribose) Polymerases (EC 2.4.2.30) ; RNA, Messenger ; CNOT1 protein, human ; Transcription Factors
Language	English
Publishing date	2024-03-31
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms25073895
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Article ; Online: Despite its sequence identity with canonical H4, Drosophila H4r product is enriched at specific chromatin regions.

Ábrahám, Andrea / Villányi, Zoltán / Zsindely, Nóra / Nagy, Gábor / Szabó, Áron / Bodai, László / Henn, László / Boros, Imre M

Scientific reports

2022 Volume 12, Issue 1, Page(s) 5007

Abstract: Histone variants are different from their canonical counterparts in structure and are encoded by solitary genes with unique regulation to fulfill tissue or differentiation specific functions. A single H4 variant gene (His4r or H4r) that is located ... ...

Abstract	Histone variants are different from their canonical counterparts in structure and are encoded by solitary genes with unique regulation to fulfill tissue or differentiation specific functions. A single H4 variant gene (His4r or H4r) that is located outside of the histone cluster and gives rise to a polyA tailed messenger RNA via replication-independent expression is preserved in Drosophila strains despite that its protein product is identical with canonical H4. In order to reveal information on the possible role of this alternative H4 we epitope tagged endogenous H4r and studied its spatial and temporal expression, and revealed its genome-wide localization to chromatin at the nucleosomal level. RNA and immunohistochemistry analysis of H4r expressed under its cognate regulation indicate expression of the gene throughout zygotic and larval development and presence of the protein product is evident already in the pronuclei of fertilized eggs. In the developing nervous system a slight disequibrium in H4r distribution is observable, cholinergic neurons are the most abundant among H4r-expressing cells. ChIP-seq experiments revealed H4r association with regulatory regions of genes involved in cellular stress response. The data presented here indicate that H4r has a variant histone function.
MeSH term(s)	Animals ; Chromatin/genetics ; Drosophila/genetics ; Histones/genetics ; Nucleosomes ; Receptors, Histamine H4/genetics
Chemical Substances	Chromatin ; Histones ; Nucleosomes ; Receptors, Histamine H4
Language	English
Publishing date	2022-03-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-022-09026-x
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Article ; Online: Despite its sequence identity with canonical H4, Drosophila H4r product is enriched at specific chromatin regions

Andrea Ábrahám / Zoltán Villányi / Nóra Zsindely / Gábor Nagy / Áron Szabó / László Bodai / László Henn / Imre M. Boros

Scientific Reports, Vol 12, Iss 1, Pp 1-

2022 Volume 11

Abstract: Abstract Histone variants are different from their canonical counterparts in structure and are encoded by solitary genes with unique regulation to fulfill tissue or differentiation specific functions. A single H4 variant gene (His4r or H4r) that is ... ...

Abstract	Abstract Histone variants are different from their canonical counterparts in structure and are encoded by solitary genes with unique regulation to fulfill tissue or differentiation specific functions. A single H4 variant gene (His4r or H4r) that is located outside of the histone cluster and gives rise to a polyA tailed messenger RNA via replication-independent expression is preserved in Drosophila strains despite that its protein product is identical with canonical H4. In order to reveal information on the possible role of this alternative H4 we epitope tagged endogenous H4r and studied its spatial and temporal expression, and revealed its genome-wide localization to chromatin at the nucleosomal level. RNA and immunohistochemistry analysis of H4r expressed under its cognate regulation indicate expression of the gene throughout zygotic and larval development and presence of the protein product is evident already in the pronuclei of fertilized eggs. In the developing nervous system a slight disequibrium in H4r distribution is observable, cholinergic neurons are the most abundant among H4r-expressing cells. ChIP-seq experiments revealed H4r association with regulatory regions of genes involved in cellular stress response. The data presented here indicate that H4r has a variant histone function.
Keywords	Medicine ; R ; Science ; Q
Subject code	570
Language	English
Publishing date	2022-03-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: Mutations in the

Collart, Martine A / Kassem, Sari / Villanyi, Zoltan

Frontiers in genetics

2017 Volume 8, Page(s) 61

Abstract: ... ...

Abstract	The
Language	English
Publishing date	2017-05-22
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2606823-0
ISSN	1664-8021
ISSN	1664-8021
DOI	10.3389/fgene.2017.00061
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Article ; Online: Phase-separated ribosome-nascent chain complexes in genotoxic stress response.

Németh-Szatmári, Orsolya / Nagy-Mikó, Bence / Györkei, Ádám / Varga, Dániel / Kovács, Bálint Barna H / Igaz, Nóra / Bognár, Bence / Rázga, Zsolt / Nagy, Gábor / Zsindely, Nóra / Bodai, László / Papp, Balázs / Erdélyi, Miklós / Kiricsi, Mónika / Blastyák, András / Collart, Martine A / Boros, Imre M / Villányi, Zoltán

RNA (New York, N.Y.)

2023 Volume 29, Issue 10, Page(s) 1557–1574

Abstract: Assemblysomes are EDTA- and RNase-resistant ribonucleoprotein (RNP) complexes of paused ribosomes with protruding nascent polypeptide chains. They have been described in yeast and human cells for the proteasome subunit Rpt1, and the disordered amino- ... ...

Abstract	Assemblysomes are EDTA- and RNase-resistant ribonucleoprotein (RNP) complexes of paused ribosomes with protruding nascent polypeptide chains. They have been described in yeast and human cells for the proteasome subunit Rpt1, and the disordered amino-terminal part of the nascent chain was found to be indispensable for the accumulation of the Rpt1-RNP into assemblysomes. Motivated by this, to find other assemblysome-associated RNPs we used bioinformatics to rank subunits of
MeSH term(s)	Humans ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; RecQ Helicases/genetics ; Edetic Acid/metabolism ; DNA Damage ; RNA/metabolism ; Ribonucleoproteins/genetics ; Ribosomes/genetics ; Ribosomes/metabolism
Chemical Substances	Saccharomyces cerevisiae Proteins ; RecQ Helicases (EC 3.6.4.12) ; Edetic Acid (9G34HU7RV0) ; RNA (63231-63-0) ; Ribonucleoproteins ; SGS1 protein, S cerevisiae (EC 3.6.1.-)
Language	English
Publishing date	2023-07-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1241540-6
ISSN	1469-9001 ; 1355-8382
ISSN (online)	1469-9001
ISSN	1355-8382
DOI	10.1261/rna.079755.123
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Article ; Online: Building on the Ccr4-Not architecture.

Villanyi, Zoltan / Collart, Martine A

BioEssays : news and reviews in molecular, cellular and developmental biology

2016 Volume 38, Issue 10, Page(s) 997–1002

Abstract: In a recent issue of Nature Communications Ukleja and co-workers reported a cryo-EM 3D reconstruction of the Ccr4-Not complex from Schizosaccharomyces pombe with an immunolocalization of the different subunits. The newly gained architectural knowledge ... ...

Abstract	In a recent issue of Nature Communications Ukleja and co-workers reported a cryo-EM 3D reconstruction of the Ccr4-Not complex from Schizosaccharomyces pombe with an immunolocalization of the different subunits. The newly gained architectural knowledge provides cues to apprehend the functional diversity of this major eukaryotic regulator. Indeed, in the cytoplasm alone, Ccr4-Not regulates translational repression, decapping and deadenylation, and the Not module additionally plays a positive role in translation. The spatial distribution of the subunits within the structure is compatible with a model proposing that the Ccr4-Not complex interacts with the 5' and 3' ends of target mRNAs, allowing different functional modules of the complex to act at different stages of the translation process, possibly within a circular constellation of the mRNA. This work opens new avenues, and reveals important gaps in our understanding regarding structure and mode of function of the Ccr4-Not complex that need to be addressed in the future.
MeSH term(s)	Cytoplasm ; Gene Expression Regulation ; RNA, Messenger/genetics ; Schizosaccharomyces/genetics
Chemical Substances	RNA, Messenger
Language	English
Publishing date	2016-10
Publishing country	United States
Document type	Journal Article
ZDB-ID	50140-2
ISSN	1521-1878 ; 0265-9247
ISSN (online)	1521-1878
ISSN	0265-9247
DOI	10.1002/bies.201600051
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Zs.A 2024: Show issues

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Article ; Online: Not5-dependent co-translational assembly of Ada2 and Spt20 is essential for functional integrity of SAGA.

Kassem, Sari / Villanyi, Zoltan / Collart, Martine A

Nucleic acids research

2017 Volume 45, Issue 12, Page(s) 7539

Language	English
Publishing date	2017-08-30
Publishing country	England
Document type	Journal Article ; Published Erratum
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkx447
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Article: Building on the Ccr4âNot architecture

Villanyi, Zoltan / Martine A. Collart

BioEssays. 2016 Oct., v. 38, no. 10

2016

Abstract: In a recent issue of Nature Communications Ukleja and coâworkers reported a cryoâEM 3D reconstruction of the Ccr4âNot complex from Schizosaccharomyces pombe with an immunolocalization of the different subunits. The newly gained architectural ... ...

Abstract	In a recent issue of Nature Communications Ukleja and coâworkers reported a cryoâEM 3D reconstruction of the Ccr4âNot complex from Schizosaccharomyces pombe with an immunolocalization of the different subunits. The newly gained architectural knowledge provides cues to apprehend the functional diversity of this major eukaryotic regulator. Indeed, in the cytoplasm alone, Ccr4âNot regulates translational repression, decapping and deadenylation, and the Not module additionally plays a positive role in translation. The spatial distribution of the subunits within the structure is compatible with a model proposing that the Ccr4âNot complex interacts with the 5â² and 3â² ends of target mRNAs, allowing different functional modules of the complex to act at different stages of the translation process, possibly within a circular constellation of the mRNA. This work opens new avenues, and reveals important gaps in our understanding regarding structure and mode of function of the Ccr4âNot complex that need to be addressed in the future.
Keywords	Schizosaccharomyces pombe ; cytoplasm ; functional diversity ; messenger RNA ; models ; translation (genetics)
Language	English
Dates of publication	2016-10
Size	p. 997-1002.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	JOURNAL ARTICLE
ZDB-ID	50140-2
ISSN	1521-1878 ; 0265-9247
ISSN (online)	1521-1878
ISSN	0265-9247
DOI	10.1002/bies.201600051
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Article ; Online: Ccr4-Not is at the core of the eukaryotic gene expression circuitry.

Villanyi, Zoltan / Collart, Martine A

Biochemical Society transactions

2015 Volume 43, Issue 6, Page(s) 1253–1258

Abstract: In this mini-review, we summarize our current knowledge about the cross-talk between the different levels of gene expression. We introduce the Ccr4 (carbon catabolite repressed 4)-Not (negative on TATA-less) complex as a candidate to be a master ... ...

Abstract	In this mini-review, we summarize our current knowledge about the cross-talk between the different levels of gene expression. We introduce the Ccr4 (carbon catabolite repressed 4)-Not (negative on TATA-less) complex as a candidate to be a master regulator that orchestrates between the different levels of gene expression. An integrated view of the findings about the Ccr4-Not complex suggests that it is involved in gene expression co-ordination. Since the discovery of the Not proteins in a selection for transcription regulators in yeast [Collart and Struhl (1994) Genes Dev. 8: , 525-537], the Ccr4-Not complex has been connected to every step of the mRNA lifecycle. Moreover, it has been found to be relevant for appropriate protein folding and quaternary protein structure by being involved in co-translational protein complex assembly.
MeSH term(s)	Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Eukaryotic Cells/metabolism ; Gene Expression Regulation ; Models, Genetic ; Multiprotein Complexes/genetics ; Multiprotein Complexes/metabolism ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; Ribonucleases/genetics ; Ribonucleases/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism
Chemical Substances	CDC36 protein, S cerevisiae ; CDC39 protein, S cerevisiae ; Cell Cycle Proteins ; Multiprotein Complexes ; RNA, Messenger ; Repressor Proteins ; Saccharomyces cerevisiae Proteins ; Transcription Factors ; CCR4 protein, S cerevisiae (EC 3.1.-) ; Ribonucleases (EC 3.1.-)
Language	English
Publishing date	2015-12
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST20150167
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