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Pang, Q.

Publications and source records attributed to Pang, Q..

6 recordsLinked to original sources

RNA m6A Methylation Control Salt Response by Affecting Photosynthesis Capacity

Soil salinization is a major abiotic stress constraining global plant growth. Epigenetic regulation particularly RNA modifications like N6-methyladenosine (m6A) is crucial for plant stress responses, the specific role of m6A in salt tolerance remains unclearly defined. Here, we show that Arabidopsis mutants deficient in m6A writers or readers exhibit heightened salt sensitivity at both growth and physiological levels. Global m6A modification levels increase following salt stress which results in a significant elevation of m6A signature throughout the Arabidopsis transcriptome. Spatiotemporal analysis through standardized read density of MeRIP-seq uncovered a significant salt-induced redistribution of m6A modification patterns. More than 80% m6A reads locate around the stop codon within 3-untranslated regions and tend to increase under salt stress. A total of 9,986 peaks aligned into 8,667 coding gene showing significant changes in m6A modification levels. By associating with gene expression profiling, 840 salt-responsive genes display significant alterations in m6A enriched level and negative regulation pattern happens in most of genes. The salt responsive genes showing increased m6A methylation but significantly decreased expression are focused which representatively enriched in photosynthesis pathway, and this suppression due to mRNA decay mediated by m6A modification. Photosynthetic capacity and chloroplast apparatus are impaired in m6A-dependent manner under salt stress. These results clarify the biological functions of m6A modification in plant response to salinity and uncover the specific role of RNA metabolism based on dynamic change pattern of m6A modification to cope with salt stress.

plant biology↗

Tryptophanol, a novel auxin analog found in marine diatoms, enhances nitrogen assimilation

Diatoms exhibit superior competitive capacity in nitrogen assimilation, largely contributing to their growth, although the mechanisms underpinning their success have not been completely understood. Here, a non-ribosomal peptide synthase-like (PtNRPS1, with an unusual domain structure A-T-R1-R2) gene was found to play a vital role in short-term nitrogen assimilation in the marine diatom Phaeodactylum tricornutum. In vitro biochemical assays and in vivo overexpression confirmed that PtNRPS1 catalyzed two sequential two-electron reductions of L-tryptophan to tryptophanol. Tryptophanol exhibits high structural and functional similarities to indole-3-acetic acid (IAA), the most typical phytohormone auxin. Surprisingly, the effective concentration of tryptophanol was lower than that of IAA by as much as 2-5 orders of magnitude for P. tricornutum. Compared with the action of IAA, a distinct molecular mode for tryptophanol was revealed by transcriptomic analysis, resulting mainly in enhanced short-term nitrogen assimilation, which was also confirmed by the elevated nitrogen uptake rates determined by stable-isotope tracking. Finally, global distribution of PtNRPS1 homologues from stramenopiles was found to be positively correlated with the abundance of genes involved in nitrogen assimilation pathways. Overall, our study provides evidence of an auxin-like derivative synthesized by an NRPS in a diatom. We speculate that tryptophanol may accelerate nitrogen assimilation, conferring advantages in the competition for nitrogen in the ocean.

plant biology↗

CSTA: A Biomarker Regulating Esophageal Stricture Epithelial Barrier, Potential Medication Target

Esophageal strictures resulting from ESD/EMR in the esophagus are distressing, with uncertain causes and treatments due to epithelial barrier dysfunction. We explored cystatin A (CSTA) as a novel biomarker for the esophageal epithelial barrier. CSTA regulates the barrier and is influenced by tacrolimus (FK506). Analyzing biopsy samples by proteomics, we identified CSTA as an esophageal epithelial biomarker. Knocking down CSTA reduced responsiveness to triamcinolone acetonide (TA) and lowered expression of proteins related to cell-cell junctions and barrier function during inflammation. These findings suggest that down-regulate CSTA weakens tight junctions and the esophageal barrier, leading to strictures. Notably, FK506 showed promise in rescuing CSTA-knockdown cells by increasing the expression of proteins related to cell-cell junctions and barrier function. This highlights FK506 as a potential therapy for esophageal strictures in patients with CSTA mutations.

cell biology↗

Histone variant H2A.Z is required for plant salt response by regulating gene transcription

As a well-conserved histone variant, H2A.Z epigenetically regulates plant growth and development as well as the interaction with environmental factors. However, the role of H2A.Z in response to salt stress remains unclear, and whether nucleosomal H2A.Z occupancy work on the gene responsiveness upon salinity is obscure. Here, we elucidate the involvement of H2A.Z in salt response by analyzing H2A.Z disorder plants with impaired or overloaded H2A.Z deposition. The salt tolerance is dramatically accompanied by H2A.Z deficiency and reacquired in H2A.Z OE lines. H2A.Z disorder changes the expression profiles of large-scale of salt responsive genes, announcing that H2A.Z is required for plant salt response. Genome-wide H2A.Z mapping shows that H2A.Z level is induced by salt condition across promoter, TSS and TES (-1 kb to +1kb), the peaks preferentially enrich at promoter regions near TSS. We further show that H2A.Z deposition within TSS provides a direct role on transcriptional control, which has both repressive and activating effects, while it is found generally H2A.Z enrichment negatively correlate with gene expression level response to salt stress. This study shed light on the H2A.Z function in salt tolerance, highlighting the complex regulatory mechanisms of H2A.Z on transcriptional activity for yielding appropriate responses to particularly environmental stress.

plant biology↗

A synergistic action of sirtuins directly recognizes DNA breaks and potentiates DNA damage response and repair

The DNA damage response (DDR) is a highly orchestrated process but how double-strand DNA breaks (DSBs) are initially recognized is unclear. Here, we show that polymerized SIRT6 deacetylase recognizes DSBs and potentiates the DDR. First, SIRT1 deacetylates SIRT6 at residue K33, which is important for SIRT6 polymerization and mobilization toward DSBs. Then, K33-deacetylated SIRT6 anchors to {gamma}H2AX, allowing its retention on and subsequent remodeling of local chromatin. We show that a K33R mutation that mimics hypoacetylated SIRT6 can rescue defective DNA repair as a result of SIRT1 deficiency in cultured cells. These data highlight the synergistic action between SIRTs in the spatiotemporal regulation of the DDR and DNA repair.

biochemistry↗

Sirt7 regulates circadian phase coherence of hepatic circadian clock via a body temperature/Hsp70-Sirt7-Cry1 axis

The biological clock is generated in the hypothalamic suprachiasmatic nucleus (SCN), which synchronizes peripheral oscillators to coordinate physiological and behavioral activities throughout the body. Disturbance of circadian phase coherence between the central and peripheral could disrupt rhythms and thus cause diseases and aging. Here, we identified hepatic Sirt7 as an early element responsive to light, which ensures the phase coherence in mouse liver. Loss of Sirt7 leads to advanced liver circadian phase; restricted feeding in daytime entrains hepatic clock more rapidly in Sirt7-/- mice compared to wild-types. Molecularly, a light-driven body temperature (BT) oscillation induces rhythmic expression of Hsp70, which binds to and promotes the ubiquitination and proteasomal degradation of Sirt7. Sirt7 rhythmically deacetylates Cry1 on K565/579 and promotes Fbxl3-mediated degradation, thus coupling hepatic clock to the central pacemaker. Together, our data identify a novel BT/Hsp70-Sirt7-Cry1 axis, which transmits biological timing cues from the central to the peripheral and ensures circadian phase coherence in livers.

molecular biology↗