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RBPL-1, the C. elegans homolog of RBBP6, promotes meiotic homolog pairing through a conserved DWNN domain

ABSTRACT: RBPL-1, the C. elegans homolog of RBBP6, promotes meiotic homolog pairing through a conserved DWNN domain

PROVIDER: PRJNA1244805 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR32938451_1.fastq.gz	Fastqsanger.gz
	SRR32938451_2.fastq.gz	Fastqsanger.gz
	SRR32938452_1.fastq.gz	Fastqsanger.gz
	SRR32938452_2.fastq.gz	Fastqsanger.gz
	SRR32938453_1.fastq.gz	Fastqsanger.gz

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RBPL-1, the C. elegans homolog of RBBP6, promotes meiotic homolog pairing through a conserved DWNN domain

Project description:Accurate chromosome segregation during meiosis depends on precise homolog pairing, a process driven by a series of specialized proteins that link chromosomes to cytoskeletal motors and coordinate chromosome movement for homolog recognition and alignment. Here, we demonstrate that RBPL-1, the C. elegans homolog of RBBP6, is necessary for normal meiotic progression, particularly for proper homolog pairing and associated nuclear reorganization. RBPL-1 is enriched on the autosomes in early and mid- pachytene nuclei. Depletion of RBPL-1 led to reduced levels of ZIM/HIM-8 family proteins and PLK-2 kinase, two critical mediators of homolog pairing. Notably, RBPL-1's role in homolog pairing is independent of the RING finger domain, which mediates ubiquitination, and its Zn knuckle domain, which is implicated in APA/mRNA processing. Instead, we reveal that the evolutionarily conserved yet functionally enigmatic DWNN domain is essential for RBPL-1's function. Our findings uncover a previously unrecognized regulatory mechanism governing homolog pairing during meiosis.

2025-04-01 | GSE293490 | GEO

Distinct intersecting pathways link homolog pairing to initiation of meiotic chromosome synapsis

Project description:Faithful meiotic segregation requires pairwise alignment of the homologous chromosomes and Synaptonemal Complex assembly (SC) at their interface. Here, we investigate on new factors that promote and coordinate these events during C. elegans meiosis. We identify BRA-2 (BMP Receptor Associated family member 2) as an interactor of HIM-17, previously shown to promote double-strand break formation. We found that loss of bra-2 specifically impairs synapsis licensing without affecting homologs recognition, SC maintenance or chromosome movement. Double mutant analysis revealed a previously unrecognized role for HIM-17 in promoting homolog pairing under dysfunctional SC assembly, without perturbing nuclear envelope recruitment of factors required for chromosome movement. We provide evidence that bra-2 and him-17 act in distinct pathways, exerting partially redundant functions in SC licensing, as well as separable roles in regulating homologs pairing. Altogether, our findings unveil novel mechanisms that ensure stabilization of homologous chromosome interaction via SC licensing upon homology assessment.

2025-03-14 | PXD053401 | Pride

MEIOC interacting proteins during meiotic prophase I

Project description:The meiosis-specific chromosomal events of homolog pairing, synapsis, and recombination occur over an extended meiotic prophase I. In this study, we show that, in mice, maintenance of an extended meiotic prophase I requires the gene Meioc, a germ-cell specific factor conserved in most metazoans. Using immunoprecipitation and quantitative mass spectrometry, we identify proteins that interact with MEIOC in the mouse germ line.

2017-03-27 | PXD005473 | Pride

A conserved seed-pairing domain affords small RNA-mediated stress resistance in enterobacteria

Project description:A conserved seed-pairing domain affords small RNA-mediated stress resistance in enterobacteria

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Highly structured homolog pairing reflects functional organization of the Drosophila genome

Project description:Trans-homolog interactions encompass potent regulatory functions, which have been studied extensively in Drosophila, where homologs are paired in somatic cells and pairing-dependent gene regulation, or transvection, is well-documented. Nevertheless, the structure of pairing and whether its functional impact is genome-wide have eluded analysis. Accordingly, we generated a diploid cell line from divergent parents and applied haplotype-resolved Hi-C, discovering that homologs pair relatively precisely genome-wide in addition to establishing trans-homolog domains and compartments. We also elucidated the structure of pairing with unprecedented detail, documenting significant variation across the genome. In particular, we characterized two forms: tight pairing, consisting of contiguous small domains, and loose pairing, consisting of single larger domains. Strikingly, active genomic regions (A-type compartments, active chromatin, expressed genes) correlated with tight pairing, suggesting that pairing has a functional role genome-wide. Finally, using RNAi and haplotype-resolved Hi-C, we show that disruption of pairing-promoting factors results in global changes in pairing.

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3D genome remodeling and homologous pairing during meiotic prophase of mouse oogenesis and spermatogenesis

Project description:We comprehensively compared the chromatin structures and transcriptomes in successive substages of female and male mouse meiotic prophase by using sisHi-C and RNA-Seq methods. Interestingly, the transcriptional change happened earlier than chromatin structures reprograming that chromatin structures largely maintained the pre-meiotic condition in leptotene. Also, compartments and TADs gradually disappeared and then slowly recovered in both oocytes and spermatocytes. We characterized the events of homologous chromosomes pairing and found homologues adopted two sex-conserved pairing strategies prior to and after leptotene-to-zygotene transition, which firstly contacted more frequently in LINE enriched compartment B and then switched to SINE enriched compartment A. The sexual difference of transcriptome was most obvious in late meiotic prophase, which reflected in gamete morphology and function differences. We also complemented marker genes for each substage of oocytes and spermatocytes meiotic prophase, and predicted the sex-specific meiotic functional genes, whose mutation or deletion may cause sex different effects on fertility. In summary, this study revealed the sexual similarities and dimorphic of higher-order chromatin architecture, homologous pairing and transcriptome during meiotic prophase of both oogenesis and spermatogenesis.

2023-09-23 | GSE220303 | GEO

Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability

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Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability

Project description:Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability

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Centromere Pairing Enables Correct Segregation of Meiotic Chromosomes

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Plant BCL-DOMAIN HOMOLOG proteins play a conserved role in SWI/SNF complex stability

Project description:The SWItch/Sucrose Non-Fermenting (SWI/SNF) complexes are evolutionarily conserved, ATP-dependent chromatin remodelers crucial for multiple nuclear functions in eukaryotes. Recently, plant BCL-Domain Homolog (BDH) proteins were identified as shared subunits of all plant SWI/SNF complexes, significantly impacting chromatin accessibility and various developmental processes in Arabidopsis. In this study, we performed a comprehensive characterization of bdh mutants, revealing a previously overlooked impact on hypocotyl cell elongation. Through detailed analysis of BDH domains, we identified a plant-specific N-terminal domain that facilitates the interaction between BDH and the rest of the complex. Additionally, we uncovered the critical role of the BDH β-hairpin domain, which is phylogenetically related to metazoan BCL7 SWI/SNF subunits. While phylogenetic analyses did not identify BDH/BCL7 orthologs in fungi, structure prediction modeling demonstrated strong similarities between the SWI/SNF catalytic modules of plants, animals, and fungi, and revealed the yeast Rtt102 protein as a structural homolog of BDH and BCL7. This finding is supported by the ability of Rtt102 to interact with the Arabidopsis catalytic module subunit ARP7 and partially rescue the bdh mutant phenotypes. Further experiments revealed that BDH promotes the stability of the ARP4-ARP7 heterodimer, leading to the partial destabilization of ARP4 in the SWI/SNF complexes. In summary, our study unveils the molecular function of BDH proteins in plant SWI/SNF complexes and suggests that β-hairpin-containing proteins are evolutionarily conserved subunits crucial for ARP heterodimer stability and SWI/SNF activity across eukaryotes.

2024-10-10 | GSE268510 | GEO

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