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Molecular Metabolisms and Regulations of Algae
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Molecular Metabolisms and Regulations of Algae

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Plant Sciences".

Deadline for manuscript submissions: 31 August 2024 | Viewed by 4251

Special Issue Editor

Prof. Dr. Elena Ermilova

E-Mail Website
Guest Editor
Biological Faculty, Saint-Petersburg State University, Saint-Petersburg 199034, Russia
Interests: green and red algae; nitrogen metabolism; nitric oxide; S-nitrosation; PII proteins; stress responses

Special Issue Information

Dear Colleagues,

Eukaryotic algae are remarkably diverse in terms of habitat, morphology, physiology, and biochemistry, and they play a critical role in global ecology. Algae are useful models for studying metabolic processes in photosynthetic organisms and potential renewable platforms for the production of beneficial chemicals. Algae adapt to various environmental conditions by changing many aspects, from gene expression to cell physiology and morphology, through the regulation of primary and secondary metabolism. Characterizing algal metabolism and its regulation is the key to understanding their role in the environment and unlocking their potential for biotechnology applications.

This Special Issue provides an open platform for the discussion of recent developments in this field, focusing on novel aspects of molecular metabolism in algae, from genes regulation and signal pathways to protein modification and enzyme activity control.

Original papers, review articles, and perspectives from experts in the field are welcome.

Prof. Dr. Elena Ermilova
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • algal enzymes
  • metabolic pathways
  • information-processing proteins
  • signal molecules and transducers
  • central metabolism
  • secondary metabolism
  • anaerobic metabolism
  • fermentation
  • omics technologies
  • biofuel production
  • protein post-translational modifications

Published Papers (4 papers)

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Research

21 pages, 3632 KiB  
Article
Differential Expression of Stress Adaptation Genes in a Diatom Ulnaria acus under Different Culture Conditions
by Elvira Bayramova, Darya Petrova, Artyom Marchenkov, Alexey Morozov, Yuri Galachyants, Yulia Zakharova, Yekaterina Bedoshvili and Yelena Likhoshway
Int. J. Mol. Sci. 2024, 25(4), 2314; https://doi.org/10.3390/ijms25042314 - 15 Feb 2024
Viewed by 797
Abstract
Diatoms are a group of unicellular eukaryotes that are essential primary producers in aquatic ecosystems. The dynamic nature of their habitat necessitates a quick and specific response to various stresses. However, the molecular mechanisms of their physiological adaptations are still underexplored. In this [...] Read more.
Diatoms are a group of unicellular eukaryotes that are essential primary producers in aquatic ecosystems. The dynamic nature of their habitat necessitates a quick and specific response to various stresses. However, the molecular mechanisms of their physiological adaptations are still underexplored. In this work, we study the response of the cosmopolitan freshwater diatom Ulnaria acus (Bacillariophyceae, Fragilariophycidae, Licmophorales, Ulnariaceae, Ulnaria) in relation to a range of stress factors, namely silica deficiency, prolonged cultivation, and interaction with an algicidal bacterium. Fluorescent staining and light microscopy were used to determine the physiological state of cells under these stresses. To explore molecular reactions, we studied the genes involved in the stress response—type III metacaspase (MC), metacaspase-like proteases (MCP), death-specific protein (DSP), delta-1-pyrroline-5-carboxylate dehydrogenase (ALDH12), and glutathione synthetase (GSHS). We have described the structure of these genes, analyzed the predicted amino acid sequences, and measured their expression dynamics in vitro using qRT-PCR. We demonstrated that the expression of UaMC1, UaMC3, and UaDSP increased during the first five days of silicon starvation. On the seventh day, it was replaced with the expression of UaMC2, UaGSHS, and UaALDH. After 45 days of culture, cells stopped growing, and the expression of UaMC1, UaMC2, UaGSHS, and UaDSP increased. Exposure to an algicidal bacterial filtrate induced a higher expression of UaMC1 and UaGSHS. Thus, we can conclude that these proteins are involved in diatoms’ adaptions to environmental changes. Further, these data show that the molecular adaptation mechanisms in diatoms depend on the nature and exposure duration of a stress factor. Full article
(This article belongs to the Special Issue Molecular Metabolisms and Regulations of Algae)
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20 pages, 5362 KiB  
Article
The Alga Uronema belkae Has Two Structural Types of [FeFe]-Hydrogenases with Different Biochemical Properties
by Ghazal Alavi, Vera Engelbrecht, Anja Hemschemeier and Thomas Happe
Int. J. Mol. Sci. 2023, 24(24), 17311; https://doi.org/10.3390/ijms242417311 - 09 Dec 2023
Viewed by 909
Abstract
Several species of microalgae can convert light energy into molecular hydrogen (H2) by employing enzymes of early phylogenetic origin, [FeFe]-hydrogenases, coupled to the photosynthetic electron transport chain. Bacterial [FeFe]-hydrogenases consist of a conserved domain that harbors the active site cofactor, the [...] Read more.
Several species of microalgae can convert light energy into molecular hydrogen (H2) by employing enzymes of early phylogenetic origin, [FeFe]-hydrogenases, coupled to the photosynthetic electron transport chain. Bacterial [FeFe]-hydrogenases consist of a conserved domain that harbors the active site cofactor, the H-domain, and an additional domain that binds electron-conducting FeS clusters, the F-domain. In contrast, most algal hydrogenases characterized so far have a structurally reduced, so-termed M1-type architecture, which consists only of the H-domain that interacts directly with photosynthetic ferredoxin PetF as an electron donor. To date, only a few algal species are known to contain bacterial-type [FeFe]-hydrogenases, and no M1-type enzymes have been identified in these species. Here, we show that the chlorophycean alga Uronema belkae possesses both bacterial-type and algal-type [FeFe]-hydrogenases. Both hydrogenase genes are transcribed, and the cells produce H2 under hypoxic conditions. The biochemical analyses show that the two enzymes show features typical for each of the two [FeFe]-hydrogenase types. Most notable in the physiological context is that the bacterial-type hydrogenase does not interact with PetF proteins, suggesting that the two enzymes are integrated differently into the alga’s metabolism. Full article
(This article belongs to the Special Issue Molecular Metabolisms and Regulations of Algae)
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16 pages, 4559 KiB  
Article
Effects of Lipids and Type of Amino Acid in Protein in Microalgae on Nitrogen Reaction Pathways during Hydrothermal Liquefaction
by Tianyi Bao, Jesse Zhu, Nianze Zhang and Yuanyuan Shao
Int. J. Mol. Sci. 2023, 24(19), 14967; https://doi.org/10.3390/ijms241914967 - 06 Oct 2023
Viewed by 1147
Abstract
It is meaningful to understand the conversion pathways of nitrogen during the hydrothermal liquefaction process of microalgae to reveal the related reaction mechanisms and develop effective methods to prevent N from ending in biocrude, which eventually increases the quality of biocrude. Extending from [...] Read more.
It is meaningful to understand the conversion pathways of nitrogen during the hydrothermal liquefaction process of microalgae to reveal the related reaction mechanisms and develop effective methods to prevent N from ending in biocrude, which eventually increases the quality of biocrude. Extending from our previous works that mainly focused on two high-protein (>50 wt%) microalgae (Chlorella sp. and Spirulina sp.), Nannochloropsis sp., which has a high lipid content (>70 wt%), was used as the feedstock for this project using the same methodology. The high lipid content in Na. induced less nitrogen during the oil phase and as a result, reduced the heteroatom content while also improving the quality of biocrude. It is worth noting that another investigation was conducted on the model compounds with different types of amino acids to specify the effects of the types of amino acids in the proteins in microalgae on the N pathway and their distribution in the products (aqueous phase, oil, solid, and gas). It was found that the basic amino acid in microalgae caused the formation of more N-heterocyclic compounds in the biocrude. The mass flow based on the mass balance was demonstrated to further refine the map showing the predicted reaction pathway of nitrogen from the previous version. Full article
(This article belongs to the Special Issue Molecular Metabolisms and Regulations of Algae)
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13 pages, 4780 KiB  
Article
N-Acetyl-L-glutamate Kinase of Chlamydomonas reinhardtii: In Vivo Regulation by PII Protein and Beyond
by Vitalina Vlasova, Tatiana Lapina, Vladislav Statinov and Elena Ermilova
Int. J. Mol. Sci. 2023, 24(16), 12873; https://doi.org/10.3390/ijms241612873 - 17 Aug 2023
Viewed by 757
Abstract
N-Acetyl-L-glutamate kinase (NAGK) catalyzes the rate-limiting step in the ornithine/arginine biosynthesis pathway in eukaryotic and bacterial oxygenic phototrophs. NAGK is the most highly conserved target of the PII signal transduction protein in Cyanobacteria and Archaeplastida (red algae and Chlorophyta). However, there is still [...] Read more.
N-Acetyl-L-glutamate kinase (NAGK) catalyzes the rate-limiting step in the ornithine/arginine biosynthesis pathway in eukaryotic and bacterial oxygenic phototrophs. NAGK is the most highly conserved target of the PII signal transduction protein in Cyanobacteria and Archaeplastida (red algae and Chlorophyta). However, there is still much to be learned about how NAGK is regulated in vivo. The use of unicellular green alga Chlamydomonas reinhardtii as a model system has already been instrumental in identifying several key regulation mechanisms that control nitrogen (N) metabolism. With a combination of molecular-genetic and biochemical approaches, we show the existence of the complex CrNAGK control at the transcriptional level, which is dependent on N source and N availability. In growing cells, CrNAGK requires CrPII to properly sense the feedback inhibitor arginine. Moreover, we provide primary evidence that CrPII is only partly responsible for regulating CrNAGK activity to adapt to changing nutritional conditions. Collectively, our results suggest that in vivo CrNAGK is tuned at the transcriptional and post-translational levels, and CrPII and additional as yet unknown factor(s) are integral parts of this regulation. Full article
(This article belongs to the Special Issue Molecular Metabolisms and Regulations of Algae)
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