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Histidine-dependent protein methylation is required for compartmentalization of CTP synthase

ABSTRACT: Histidine-dependent protein methylation is required for compartmentalization of CTP synthase

PROVIDER: PRJNA415056 | ENA |

REPOSITORIES: ENA

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Histidine-dependent protein methylation is required for compartmentalization of CTP synthase

Project description:CTP synthase (CTPS) forms compartmentalized filaments in response to substrate availability and environmental nutrient status. However, the physiological role of filaments and mechanisms for filament assembly are not well understood. Here, we provide evidence that CTPS forms filaments in response to histidine influx during glutamine starvation. CTPS protein levels remained stable in the presence of histidine during nutrient deprivation, followed by rapid cell growth following nutrient replenishment. Tetramer conformation-based filament formation restricted CTPS enzyme activity duringnutrient deprivation. Furthermore, we demonstrated that filament formation controlled at two levels. Starvation stress/glutamine deficiency activates the GCN2/ATF4/MTHFD2 axis to accelerate the folate cycle in mitochondria for energy homeostasis. In addition, histidine promotes re-methylation of homocysteine by donating one-carbon to the cytosolic folate cycle. CTPS filament formation induced by histidine-mediated methylation maybe a strategy usedby cancer cells to maintain homeostasis and ensure a growth advantage in adverse environments.

2018-08-29 | GSE105251 | GEO

Identification of CTPS1 Filament Interacting Proteins

Project description:CTP synthase (CTPS) catalyzes the formation of CTP in de novo pyrimidine biosynthesis pathway. Compartmentalization of CTPS into filamentous structure is evolutionarily conserved from E.coli, yeast, Drosophila, mice to humans. Recently, we have demonstrated that histidine-mediated protein methylation promotes the formation of CTPS filament under glutamine and/or serum deprivation, which reduces its enzymatic activity and protects it from degradation. However, it is still unclear how the filament assembly takes place. In the current study, we used APEX2-mediated in vivo proximity labeling to identify proteins involved in CTPS filament formation.

2020-03-24 | PXD010921 | Pride

Identification of CTPS1 Filament Interacting Proteins_2019 dataset

Project description:CTP synthase (CTPS) catalyzes the formation of CTP in de novo pyrimidine biosynthesis pathway. Compartmentalization of CTPS into filamentous structure is evolutionarily conserved from E.coli, yeast, Drosophila, mice to humans. Previously, we demonstrated that histidine (His) mediated methylation promotes the formation of CTPS filament to suppress the enzymatic activity and preserve CTPS protein under Gln deprivation, which promotes cancer cell growth after stress alleviation. However, it remains unclear where and how these enigmatic structures are assembled. Here we used APEX2-mediated in vivo proximity labeling to identify proteins involve in the formation of human CTPS filaments.

2020-03-24 | PXD015507 | Pride

Histidine re-sensitizes acute lymphoblastic leukemia cells to 6-mercaptopurine through tetrahydrofolate consumption and SIRT5-mediated desuccinylation

Project description:Given the progressive improvements in the efficacy of multiagent chemotherapy and the survival rate of pediatric acute lymphoblastic leukemia (ALL), concerted efforts are required to eradicate chemoresistance-induced disease progression and relapse. Our present study coupled chemoresistance in B-ALL with histidine metabolism deficiency. We provide evidence that histidine supplementation significantly shifts the 6-MP dose response in 6-MP-resistant B-ALL cell lines and xenograft mice model. Moreover, we prove that the THF consumption through histidine degradation pathway and SIRT5-mediated desuccinylation of HINT1 are required for the histidine combination therapy to promote B-ALL cells against 6-MP resistance. Collectively, our results demonstrated that histidine supplementation and SIRT5-HINT1 axis activators might be rational strategies to overcome chemoresistance, thus protect B-ALL patients from disease progression or recurrence.

2023-07-27 | GSE236934 | GEO

WGS histidine overproducers

Project description:Whole genomes sequencing to determine mutations in histidine overproducers generated with a toxic histidine analog

| PRJEB45772 | ENA

A molecular mechanism for compartmentalization and silencing of chromatin domains at the nuclear lamina

Project description:This SuperSeries is composed of the following subset Series: GSE35777: A molecular mechanism for compartmentalization and silencing of chromatin domains at the nuclear lamina [Tiling Array] GSE36048: A molecular mechanism for compartmentalization and silencing of chromatin domains at the nuclear lamina [ChIP-seq] Refer to individual Series

2012-02-24 | E-GEOD-36049 | biostudies-arrayexpress

Studying the effects of endogenous and exogenous histidine supplementation on Pichia pastoris cultured in YPA

Project description:A histidine prototrophic strain achieves A600 three-four fold higher than a histidine auxotroph when cultured in nutrient rich media YPA, which is abundant in amino acids. This retaded growth of histidine auxotroph in YPA can also be rescued by supplementing media with exogenous histidine. Here, we aim to study the transcriptomic changes associated with culturing of histidine auxotroph and prototroph in YPA and also the effects of histidine addition to the culture medium of histidine auxotroph.

2022-04-06 | GSE174633 | GEO

ADHERENT1 IS A 3-KETOACYL CoA SYNTHASE REQUIRED FOR MAIZE CUTICLE DEVELOPMENT AND ORGAN SEPARATION

Project description:ADHERENT1 IS A 3-KETOACYL CoA SYNTHASE REQUIRED FOR MAIZE CUTICLE DEVELOPMENT AND ORGAN SEPARATION

| PRJNA598606 | ENA

Widespread protein histidine phosphorylation in bacteria

Project description:For decades, extreme difficulties in analyzing histidine phosphorylation have limited the study of phosphohistidine signaling. Here we report a method revealing widespread and abundant protein histidine phosphorylation in E. coli. Our new approach generated the largest E. coli phosphoproteome dataset to date, of which a remarkable high percentage (~10%) are phosphohistidine sites. This resource enables a major step forward towards a better understanding of the biological function of histidine phosphorylation.

2017-12-07 | PXD008369 | JPOST Repository

SETD3-mediated histidine methylation of MCM7 regulates DNA replication by facilitating chromatin loading of MCM

Project description:The minichromosome maintenance complex (MCM) DNA helicase is an important replicative factor during DNA replication. The proper chromatin loading of MCM is a key step to ensure replication initiation during G1/S phase. Because replication initiation is regulated by multiple biological cues, additional changes to MCM may provide deeper understanding towards this event. Here, we uncover that the histidine methyltransferase SETD3 promotes DNA replication in an enzymatic activity dependent manner. Nascent-strand sequencing (NS-seq) shows that SETD3 regulates replication initiation, as depletion of SETD3 attenuates early replication origins firing. Mechanistically, biochemical experiments reveal that SETD3 binds MCM mainly during G1/S phase, which is required for CDT1-mediated chromatin loading of MCM. The MCM loading relies on the histidine-459 methylation (H459me) on MCM7 that is catalyzed by SETD3. Impairment of H459 methylation attenuates DNA synthesis and chromatin loading of MCM. Furthermore, we show that CDK2 phosphorylates SETD3 at Serine-21 during the G1/S phase, which is required for DNA replication and cell cycle progression. These findings demonstrate a novel mechanism by which SETD3 methylates MCM to regulate replication initiation.

2024-03-12 | GSE243937 | GEO

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