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Nuclear functions of KaeA, the subunit of KEOPS complex in Aspergillus nidulans

ABSTRACT: Nuclear functions of KaeA, the subunit of KEOPS complex in Aspergillus nidulans

PROVIDER: PRJNA852546 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR19845301_1.fastq.gz	Fastqsanger.gz
	SRR19845301_2.fastq.gz	Fastqsanger.gz
	SRR19845302_1.fastq.gz	Fastqsanger.gz
	SRR19845302_2.fastq.gz	Fastqsanger.gz
	SRR19845303_1.fastq.gz	Fastqsanger.gz

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Nuclear functions of KaeA, the subunit of KEOPS complex in Aspergillus nidulans.

Project description:The aim of this project is to confirm that KaeA a subunit of highly conserved KEOPS/EKC complex, participates in the transcription regulation in Aspergillus nidulans. To identify genes directly or indirectly regulated by KaeA, the RNA-seq experiments were performed using kaeA mutants and the wild type kaeA+ strain.

2022-10-28 | GSE206830 | GEO

Nuclear functions of KaeA, the subunit of KEOPS complex in Aspergillus nidulans.

Project description:Nuclear functions of KaeA, the subunit of KEOPS complex in Aspergillus nidulans.

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Nuclear functions of KaeA, the subunit of KEOPS complex in Aspergillus nidulans

Project description:The aim of this project is to confirm that KaeA, the subunit of highly conserved KEOPS/EKC complex, participates in the transcription regulation in Aspergillus nidulans.The ChIP-seq experiment was performed to identify chromatin regions directly or indirectly bound by KaeA.

2022-10-28 | GSE206874 | GEO

Identification of proteins interacting with KaeA, the subunit of KEOPS complex in Aspergillus nidulans in vivo.

Project description:The Kae1/KaeA protein is a subunit of the highly evolutionarily conserved KEOPS complex (Kinase, Endopeptidase and Other Proteins of Small size). The Kae1/KaeA gene has been identified in all previously sequenced genomes of Archea, Bacteria and Eucaryota, except for the most reduced genomes. The KEOPS complex participates in the universal modification of the tRNA converting adenosine A37 to N6-threonylcarbamoyl adenosine (t6A37). This modification of A37, immediately 3’ of anticodons decoding ANN codons, is one of the few tRNA modifications present in all organisms and plays an extremely important role in the accuracy of the translation process. We characterized two mutations in kaeA of filamentous fungus Aspergillus nidulans that result in the derepression of arginine catabolic enzymes and also showed that kaeA is involved in the regulation of several other genes that control various domains of cellular metabolism. This suggests that kaeA has additional function apart from t6A37 modification. To support this hypothesis we looked for proteins interacting with KaeA.

2023-03-11 | PXD034554 | Pride

Nuclear Functions of KaeA, a Subunit of the KEOPS Complex in <i>Aspergillus nidulans</i>.

Project description:Kae1 is a subunit of the highly evolutionarily conserved KEOPS/EKC complex, which is involved in universal (t6A37) tRNA modification. Several reports have discussed the participation of this complex in transcription regulation in yeast and human cells, including our previous observations of KaeA, an Aspergillus nidulans homologue of Kae1p. The aim of this project was to confirm the role of KaeA in transcription, employing high-throughput transcriptomic (RNA-Seq and ChIP-Seq) and proteomic (LC-MS) analysis. We confirmed that KaeA is a subunit of the KEOPS complex in A. nidulans. An analysis of kaeA19 and kaeA25 mutants showed that, although the (t6A37) tRNA modification is unaffected in both mutants, they reveal significantly altered transcriptomes compared to the wild type. The finding that KaeA is localized in chromatin and identifying its protein partners allows us to postulate an additional nuclear function for the protein. Our data shed light on the universal bi-functional role of this factor and proves that the activity of this protein is not limited to tRNA modification in cytoplasm, but also affects the transcriptional activity of a number of nuclear genes. Data are available via the NCBI's GEO database under identifiers GSE206830 (RNA-Seq) and GSE206874 (ChIP-Seq), and via ProteomeXchange with identifier PXD034554 (proteomic).

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Unravelling the pathobiological role of the fungal KEOPS complex in Cryptococcus neoformans

Project description:The kinase, putative endopeptidase and other peptides of small size (KEOPS) complex plays critical cellular functions in eukaryotes, but its pathobiological roles remains elusive in fungal pathogens. Here we comprehensively analyze the pathobiological functions of the KEOPS complex in fungal meningoencephalitis pathogen Cryptococcus neoformans. The cryptococcal KEOPS complex appears to have a linear arrangement of Pcc1-Kae1-Bud32-Cgi121, supported by physical interaction between Pcc1-Kae1, Kae1-Bud32, and Bud32-Cgi121, but does not have Gon7 ortholog, which is the part of the S. cerevisiae KEOPS complex. Deletion of PCC1, KAE1, and BUD32 causes severe growth defects with perturbed cell cycle control.

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tRNA binding to KEOPS human protein complex

Project description:N6-theronylcarbomyl adenosine (t6A) is a universal tRNA posttranscriptional modification that promotes translation fidelity and is therefore required for the fitness of virtually all living cells. Kae1, the t6A modifying enzyme in eukaryotes and archea, resides within the KEOPS complex with three auxiliary subunits of unknown function namely Cgi121, Bud32 and Pcc1. Through biochemical and X-ray crystallographic analyses we show that Cgi121 functions to recruit substrate tRNA to KEOPS via its universal 3’-CCA tail. Incorporation of the Cgi121-tRNA structure into a composite model of KEOPS reveals an extended tRNA contact surface that surprisingly spans all four subunits. Comprehensive mutational and functional analyses validate the relevance of the extended tRNA-binding surface in vivo and in vivo. Together this work provides insight into the t6A catalytic cycle and its regulation through the cooperative action of all four KEOPS subunit through direct contacts with tRNA.

2020-12-11 | PXD018007 | Pride

NRDE2 negatively regulates nuclear exosome functions I

Project description:NRDE2 negatively regulates nuclear exosome functions I

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NRDE2 negatively regulates nuclear exosome functions IV

Project description:NRDE2 negatively regulates nuclear exosome functions IV

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