bioRxiv Science⌕ Search

bioRxiv · 10.1101/2024.11.20.624610

Amyloplasts are necessary for full gravitropism in thallus of Marchantia polymorpha

Abstract

Gravitropism is a response in which plants sense gravity and determine the direction of organ growth and development. This trait is important for adaptation in land plants. The molecular mechanisms of gravitropism have been studied mainly in flowering plants, but there is limited research on other organisms. In this study, we examined the gravitropic response of the liverwort Marchantia polymorpha, a model for investigating the evolution of land plants. We found the tips of the thallus extend upward and form several straight narrow structures in the dark. These growth directions were always in the opposite direction of gravity, and clinostat treatment disrupted them. The parenchymatous cells in the narrow structures contained amyloplasts, and the sedimentation of the amyloplasts preceded the gravitropic curvature, suggesting their role as statoliths. The starchless mutants, Mppgm1 and Mpaps1 were generated, and an abnormal direction of growth was observed in the narrow structures, but they tended to elongate upward. These observations indicate that although amyloplasts are required for complete gravitropism, plants can sense gravity without well-developed amyloplasts. These results suggest that land plants use amyloplasts as statoliths but also have amyloplast-independent mechanisms of gravitropism. These results suggest that land plants use amyloplasts as statoliths but also have amyloplast-independent mechanisms of gravitropism. HighlightIn M. polymorpha, amyloplasts act as statoliths in parenchyma cells and are important in gravitropism but it was not completely lost without starch granules.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Hashimoto-Sugimoto, M.. 2024-11-21. Amyloplasts are necessary for full gravitropism in thallus of Marchantia polymorpha. https://doi.org/10.1101/2024.11.20.624610

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Unraveling the metabolic landscape of alkaptonuria through a human-relevant in vitro liver disease model

Alkaptonuria (AKU) is a rare inherited metabolic disorder of tyrosine catabolism caused by a deficient homogentisate 1,2-dioxygenase (HGD) enzyme. This results in the accumulation of homogentisic acid (HGA), driving a progressive multisystem pathology characterized by debilitating early-onset osteoarthritis due to connective tissue degeneration. While previous in vitro studies have primarily relied on exogenous HGA exposure in osteoarticular cell models, the direct metabolic consequences of endogenous HGD deficiency within its native hepatic context remain poorly understood. Here, we established the first human-relevant HGD knockout hepatic in vitro model using a universal in-house-developed homology-directed repair approach. Integrative multi-omic analysis revealed that HGD deficiency induces widespread metabolic rewiring extending beyond disrupted tyrosine catabolism. HGD-deficient hepatocytes exhibited elevated oxidative stress accompanied by impaired mitochondrial respiration and a pseudohypoxic metabolic adaptation toward increased glycolytic dependency. Despite this glycolytic shift, the cells displayed reduced anabolic and translational activity alongside attenuated proliferation, consistent with a chronic stress-adaptive survival state rather than a proliferative metabolic phenotype. This study provides systems-level insights into the pathophysiology of AKU and establishes a versatile platform for mechanistic and therapeutic investigation.

cell biology↗

P-body sequestration of clock transcripts delays repressor synthesis to set circadian period in Drosophila

Negative-feedback oscillators require a delay between the accumulation of a repressor's mRNA and the action of its protein. In the circadian clock, this delay has been attributed largely to post-translational control of PERIOD (PER) stability and nuclear entry. The RNA-binding proteins shown to regulate per translation, ATAXIN2 and its partners, promote it, leaving open whether any step holds clock transcripts back before they are translated. Here, using time-resolved miniTurbo proximity labeling of endogenous PER across four phases of the circadian cycle in Drosophila clock neurons, we define a 252-protein PER proximitome that partitions into a nuclear arm and a cytoplasmic RNA-metabolism arm. A behavioral RNAi screen identified two P-body components, the DEAD-box helicase Me31B (DDX6) and the 5'-3' exonuclease Pacman (Pcm; XRN1), as strong regulators of circadian rhythms. Using single-molecule RNA-FISH, proximity RNA editing and ribosome profiling, we show that as per and tim transcripts accumulate, they localize to Me31B-labeled P-bodies and are poorly translated, most prominently at ZT12. Me31B knockdown disrupts P-bodies and releases per mRNA from them, causing PER to accumulate earlier and to ~2-fold higher levels, whereas Me31B overexpression delays PER accumulation and lengthens the free-running period by ~2 h. Knockdown of Pcm, in contrast, impairs clearance of per mRNA, sustaining PER and TIM accumulation, prolonging the repression phase and abolishing cycling of ~89% of rhythmic transcripts. Together, these findings identify P-body sequestration as a repressive step that delays repressor synthesis, and Pcm-dependent decay as required to end repression on time. Given the deep conservation of DDX6 and XRN1, RNP compartments may provide a conserved means of generating delay in circadian and other negative-feedback circuits.

cell biology↗

Defining redundancy in the stickers and spacers of the cell-cell junction protein Canoe's intrinsically disordered region

Cell-cell adherens junctions (AJs) and their dynamic cytoskeletal linkage power morphogenesis. AJs are enormous complexes with hundreds of proteins linked by multivalent interactions. Like other biomolecular condensates, intrinsically disordered regions (IDRs) in junctional proteins play important roles in AJ assembly and function, using spacer elements to span distances, and stickers to engage targets. To define molecular mechanisms, we need to define the functional units within IDRs. Drosophila Canoe, homolog of human Afadin, is our model. Canoe mediates morphogenesis and has an extensive IDR, with two conserved F-actin-binding stickers and two poorly conserved spacers. We combined biochemical, genetic and cell biological approaches to define the function of these IDR elements. While no single element is essential, deleting the full IDR essentially eliminates Canoe function. By scrambling the amino acid sequence of the spacers, we find that length and composition are more important than amino acid sequences, though sequences in the C-terminal spacer affect Canoe localization. Finally, we test redundancy of the F-actin-binding stickers. Deleting both reduces but does not eliminate viability, and sensitized assays reveal their redundant roles. These data reveal the robustness of IDRs.

cell biology↗