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Complete and manually curated giant archaeal Borg genomes from environmental metagenomic datasets

ABSTRACT: Tandem repeats in giant archaeal Borg elements undergo rapid evolution and create new intrinsically disordered regions in proteins

PROVIDER: PRJNA914281 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR22829730_1.fastq.gz	Fastqsanger.gz
	SRR22829730_2.fastq.gz	Fastqsanger.gz
	SRR22829731_1.fastq.gz	Fastqsanger.gz
	SRR22829731_2.fastq.gz	Fastqsanger.gz
	SRR22829732_1.fastq.gz	Fastqsanger.gz

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Project description:Components of the transcription machinery can undergo liquid-liquid phase separation, but the functional importance of phase-separated condensates in transcriptional control is not well understood. Here we report that disease-causing mutations in several transcription factors (TFs) alter the phase separation capacity of those TFs. We first demonstrate that the Hoxd13 TF, and its intrinsically disordered N-terminus form phase-separated condensates. Expansions of a polyalanine repeat, which cause hereditary synpolydactyly in humans, facilitate phase separation of Hoxd13, and alter the transcriptional program of several cell types in a cell-specific manner in vivo. Disease-associated expansions of aminoacid repeats in intrinsically disordered regions of other TFs were similarly found to alter phase separation. These results suggest that aberrant phase separation of transcriptional regulators may underlie a spectrum of human pathologies. The paper is available at https://doi.org/10.1016/j.cell.2020.04.018

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Project description:Short tandem repeats of human genome are intrinsically unstable in cultured cells in vivo

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Project description:Capture Seuencing of Tandem Repeats

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Recruitment of mRNAs to P granules by gelation with intrinsically-disordered proteins (RNAseq datasets)

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A giant virus genome is densely packaged by stable nucleosomes

Project description:The doublet histones of Marseillevirus are distantly related to the four eukaryotic core histones and wrap DNA to form remarkably similar nucleosomes. By releasing Marseillevirus chromatin from virions into solution and performing genome-wide nuclease digestion and chemical cleavage assays, we find that the higher-order organization of Marseillevirus chromatin differs greatly from that of eukaryotes. Marseillevirus nucleosomes fully protect DNA within virions, without linker DNA or phasing along genes. Likewise, we observe that most nucleosomes reconstituted onto 3-copy tandem repeats of a nucleosome positioning sequence are tightly packed and fully wrapped. We also document repeat generation and instability during viral passage in amoeboid culture. Dense promiscuous packing of fully wrapped nucleosomes rather than “beads-on-a-string” with genic punctuation suggests a viral genome protection function for doublet histones.

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