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Journals / Adnan Menderes Üniversitesi Ziraat Fakültesi Dergisi / 2022 / Cilt: 19 - Sayı: 2

Promiscuous Arylsulfatase Activity in Chlamydomonas reinhardtii

Chlamydomonas reinhardtii'de Seçici Olmayan Arilsülfataz Aktivitesi

Münevver AKSOY
Pages
213–218
Publication Date
2022-12-30
DOI
—
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

Our results show that C. reinhardtii ARS can hydrolyze both sulfate monoester (5-bromo-4-chloro-3 indolyl sulfate; X-SO42-) and phosphate monoester (5-bromo-4-chloro-3 indolyl phosphate; X-PO43-) providing evidence that ARS enzyme has promiscuous activity.

📌 3 Key Takeaways

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Objective & Hypothesis:Sulfate is an essential macroelement for all living organisms.
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Key Findings & Data:Our results show that C. reinhardtii ARS can hydrolyze both sulfate monoester (5-bromo-4-chloro-3 indolyl sulfate; X-SO42-) and phosphate monoester (5-bromo-4-chloro-3 indolyl phosphate; X-PO43-) providing evidence that ARS enzyme has promiscuous activity.
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Conclusion & Impact:This promiscuous activity can be beneficial in making both sulfate and phosphate bioavailable for uptake by soil organisms and plant roots.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Chlaydomonas reinhardtii · Arilsülfataz · Sülfat

Abstract

Sulfate is an essential macroelement for all living organisms. However, sulfate can be limited in agricultural settings. Microorganisms change their gene expression to acclimate to sulfate deficient conditions. Green microalga Chlamydomonas reinhardtii expresses and secretes extracellular arylsulfatase (ARS) under sulfate deficient conditions. Our results show that C. reinhardtii ARS can hydrolyze both sulfate monoester (5-bromo-4-chloro-3 indolyl sulfate; X-SO42-) and phosphate monoester (5-bromo-4-chloro-3 indolyl phosphate; X-PO43-) providing evidence that ARS enzyme has promiscuous activity. C. reinhardtii is found in soil and fresh water habitats in nature. This promiscuous activity can be beneficial in making both sulfate and phosphate bioavailable for uptake by soil organisms and plant roots.

Özet

Sülfat canlılar için zorunlu bir makroelementtir. Buna rağmen, sülfat tarımsal alanlarda eksik olabilir. Mikroorganizmalar gen ekspresyonlarını değistirerek sülfat eksikliğine aklimasyon gösterirler. Yeşil mikroalg Chlamydomonas reinhardtii sülfat eksikliği altında arilsülfataz (ARS) sentezler ve hücre dışına salgılar. Bu çalışmadaki sonuçlarımız, C. reinhardtii ARS’ın hem sülfat monoesterlerini (5-bromo-4-chloro-3 indolyl sulfate; X-SO42-) hem de fosfat monoesterlerini (5-bromo-4-chloro-3 indolyl phosphate; X-PO43-) hidrolize ettiğini göstermiştir. Bu da ARS’ın seçici olmayan aktiviteye sahip olduğuna kanıt sunmaktadır. C. reinhardtii toprak ve taze su ortamlarında yaşamaktadır. Sahip olduğu seçici olmayan ARS aktivitesi hem sülfatın hem de fosfatın bitki tarafından kullanılabilir forma getirilmesine katkı sağlayabilir.

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Cite This Article

AKSOY, M. (2022). Promiscuous Arylsulfatase Activity in Chlamydomonas reinhardtii. Adnan Menderes Üniversitesi Ziraat Fakültesi Dergisi, Cilt: 19 - Sayı: 2, 213–218. https://ajindex.com/articles/874160

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References (11)

  1. Aksoy M, Pootakham W, Pollock SV, Moseley JL, González-Ballester D, Grossman AR (2013) Tiered Regulation of Sulfur Deprivation Responses in Chlamydomonas reinhardtii and Identification of an Associated Regulatory Factor. Plant Physiology 162: 195–211.
  2. Aksoy M, Pootakham W, Grossman AR (2014) Critical Function of a Chlamydomonas reinhardtii Putative Polyphosphate Polymerase Subunit during Nutrient Deprivation. The Plant Cell 26: 4214–4229.
  3. Boltes I, Czapinska H, Kahnert A, von Bülow R, Dierks T, Schmidt B, von Figura K, Kertesz MA, Usón I (2001) 1.3 Å Structure of Arylsulfatase from Pseudomonas aeruginosa Establishes the Catalytic Mechanism of Sulfate Ester Cleavage in the Sulfatase Family. Structure 9: 483–491.
  4. Bouranis DL, Malagoli M, Avice JC, Bloem E (2020) Advances in Plant Sulfur Research. Plants 9, 256. Chruszcz M, Laidler P, Monkiewicz M, Ortlund E, Lebioda L, Lewinski K (2003) Crystal structure of a covalent intermediate of endogenous human arylsulfatase A. Journal of Inorganic Biochemistry 96: 386–392.
  5. Cloves JM, Dodgson KS, Games DE, Shaw DJ, White GF (1977) The Mechanism of Action of Primary Alkylsulphohydrolase and Arylsulphohydrolase from a Detergent-degrading Microorganism. Biochemistry Journal 167: 843–846.
  6. Davies JP, Yildiz F, Grossman AR (1994) Mutants of Chlamydomonas with Aberrant Responses to Sulfur Deprivation. The Plant Cell 6: 53–63.
  7. De Hostos EL, Togasaki RK, Grossman A (1988) Purification and Biosynthesis of a Derepressible Periplasmic Arylsulfatase from Chlamydomonas reinhardtii. Journal of Cell Biology 106: 29–37.
  8. De Hostos EL, Schilling J, Grossman AR (1989) Structure and Expression of the Gene Encoding the Periplasmic Arylsulfatase of Chlamydomonas reinhardtii. MGG Molecular & General Genetics, 218: 229–239.
  9. Dierks T, Lecca MR, Schlotterhose P, Schmidt B, von Figura K (1999) Sequence Determinants Directing Conversion of Cysteine to Formylglycine in Eukaryotic Sulfatases. EMBO Journal 18: 2084–2091.
  10. Gorman DS, Levine RP (1965) Cytochrome f and Plastocyanin: Their Sequence in the Photosynthetic Electron Transport Chain of Chlamydomonas reinhardi. Proceedings of the National Academy of Sciences of the United States of America 54(6): 1665–1669.
  11. Günal S, Hardman R, Kopriva S, Mueller JW (2019) Sulfation Pathways From Red to Green. Journal of Biological Chemistry 294(33): 12293–12312. Jonas S, van Loo B, Hyvonen M, Hollfelder F (2008) A New Member of the Alkaline Phosphatase Superfamily with a Formylglycine Nucleophile: Structural an