Feeding deterrence properties of apo-fucoxanthinoids from marine diatoms. II. Physiology of production of apo-fucoxanthinoids by the marine diatoms Phaeodactylum tricornutum and Thalassiosira pseudonana, and their feeding deterrent effects on the copepod Tigriopus californicus

1995 ◽  
Vol 124 (3) ◽  
pp. 473-481 ◽  
Author(s):  
B. A. Shaw ◽  
P. J. Harrison ◽  
R. J. Andersen
Keyword(s):  
Phaeodactylum Tricornutum ◽  
Thalassiosira Pseudonana ◽  
Feeding Deterrent ◽  
Feeding Deterrence ◽  
Marine Diatoms ◽  
Tigriopus Californicus

Feeding deterrence properties of apo-fucoxanthinoids from marine diatoms. I. Chemical structures of apo-fucoxanthinoids produced by Phaeodactylum tricornutum

1995 ◽  
Vol 124 (3) ◽  
pp. 467-472 ◽  
Author(s):  
B. A. Shaw ◽  
R. J. Andersen ◽  
P. J. Harrison
Keyword(s):  
Phaeodactylum Tricornutum ◽  
Feeding Deterrence ◽  
Marine Diatoms ◽  
Chemical Structures

Growth and competition of the marine diatoms Phaeodactylum tricornutum and Thalassiosira pseudonana. II. Light limitation

1979 ◽  
Vol 50 (4) ◽  
pp. 313-318 ◽  
Author(s):  
D. M. Nelson ◽  
C. F. D'Elia ◽  
R. R. L. Guillard
Keyword(s):  
Phaeodactylum Tricornutum ◽  
Thalassiosira Pseudonana ◽  
Light Limitation ◽  
Marine Diatoms

INTERACTION (ALLELOPATHY) BETWEEN MARINE DIATOMS: THALASSIOSIRA PSEUDONANA AND PHAEODACTYLUM TRICORNUTUM

1979 ◽  
Vol 15 (3) ◽  
pp. 353-362 ◽  
Author(s):  
Jonathan H. Sharp ◽  
Peter A. Underhill ◽  
David J. Hughes
Keyword(s):  
Phaeodactylum Tricornutum ◽  
Thalassiosira Pseudonana ◽  
Marine Diatoms

Localization of putative carbonic anhydrases in two marine diatoms, Phaeodactylum tricornutum and Thalassiosira pseudonana

2011 ◽  
Vol 109 (1-3) ◽  
pp. 205-221 ◽  
Author(s):  
Masaaki Tachibana ◽  
Andrew E. Allen ◽  
Sae Kikutani ◽  
Yuri Endo ◽  
Chris Bowler ◽  
...  
Keyword(s):  
Phaeodactylum Tricornutum ◽  
Thalassiosira Pseudonana ◽  
Carbonic Anhydrases ◽  
Marine Diatoms

INTERACTION (ALLELOPATHY) BETWEEN MARINE DIATOMS: THALASSIOSIRA PSEUDONANA AND PHAEODACTYLUM TRICORNUTUM 1

1979 ◽  
Vol 15 (4) ◽  
pp. 353-362 ◽  
Author(s):  
Jonathan H. Sharp ◽  
Peter A. Underhill ◽  
David J. Hughes
Keyword(s):  
Phaeodactylum Tricornutum ◽  
Thalassiosira Pseudonana ◽  
Marine Diatoms

Growth and competition of the marine diatoms Phaeodactylum tricornutum and Thalassiosira pseudonana. I. Nutrient effects

1979 ◽  
Vol 50 (4) ◽  
pp. 305-312 ◽  
Author(s):  
C. F. D'Elia ◽  
R. R. L. Guillard ◽  
D. M. Nelson
Keyword(s):  
Phaeodactylum Tricornutum ◽  
Thalassiosira Pseudonana ◽  
Marine Diatoms ◽  
Nutrient Effects

Influence of the Insecticide Diflubenzuron (Dimilin) on the Growth of Marine Diatoms and a Harpacticoid Copepod in Culture

1985 ◽  
Vol 42 (7) ◽  
pp. 1272-1277 ◽  
Author(s):  
N. J. Antia ◽  
P. J. Harrison ◽  
D. S. Sullivan ◽  
T. Bisalputra
Keyword(s):  
Skeletonema Costatum ◽  
Harpacticoid Copepod ◽  
Adult Survival ◽  
Thalassiosira Weissflogii ◽  
Marine Diatoms ◽  
Tigriopus Californicus ◽  
Per Se ◽  
Juvenile Development ◽  
Cyclotella Cryptica ◽  
Injurious Effects

Diflubenzuron (Dimilin) was tested, in the concentration range 0.1–5000 μg∙L−1, for possible injurious effects on the growth and photosynthesis of three chitin-producing (Thalassiosira weissflogii, T. norden-skioldii, Cyclotella cryptica) and one nonchitinaceous (Skeletonema costatum) diatoms. For comparison, the effects of the pesticide were also examined on adult survival and juvenile development of the harpacticoid copepod Tigriopus californicus. While the development of the copepod was hindered at concentrations of the order of 1–10 μg∙L−1, the diatoms were barely affected by Dimilin even at the highest concentration tested (5 mg∙L−1). We conclude that Dimilin acts specifically on insects and crustaceans as a larvicide by interfering with chitin deposition into cuticles during juvenile development through ecdysis. The lack of effect from Dimilin on the chitin-producing diatoms has suggested that the insecticide may not inhibit chitin biosynthesis per se as was previously believed, but that it presumably deregulates one or more of the larval postsynthetic processes responsible for chitin integration into cuticles.

scholarly journals The iron-sulfur scaffold protein HCF101 unveils the complexity of organellar evolution in SAR, Haptista and Cryptista

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Jan Pyrih ◽  
Vojtěch Žárský ◽  
Justin D. Fellows ◽  
Christopher Grosche ◽  
Dorota Wloga ◽  
...  
Keyword(s):  
Phylogenetic Analysis ◽  
Complex I ◽  
Phaeodactylum Tricornutum ◽  
Tetrahymena Thermophila ◽  
Thalassiosira Pseudonana ◽  
Cellular Distribution ◽  
Iron Sulfur Cluster ◽  
Iron Sulfur ◽  
Secondary Plastids ◽  
Respiratory Complex I

Abstract Background Nbp35-like proteins (Nbp35, Cfd1, HCF101, Ind1, and AbpC) are P-loop NTPases that serve as components of iron-sulfur cluster (FeS) assembly machineries. In eukaryotes, Ind1 is present in mitochondria, and its function is associated with the assembly of FeS clusters in subunits of respiratory Complex I, Nbp35 and Cfd1 are the components of the cytosolic FeS assembly (CIA) pathway, and HCF101 is involved in FeS assembly of photosystem I in plastids of plants (chHCF101). The AbpC protein operates in Bacteria and Archaea. To date, the cellular distribution of these proteins is considered to be highly conserved with only a few exceptions. Results We searched for the genes of all members of the Nbp35-like protein family and analyzed their targeting sequences. Nbp35 and Cfd1 were predicted to reside in the cytoplasm with some exceptions of Nbp35 localization to the mitochondria; Ind1was found in the mitochondria, and HCF101 was predicted to reside in plastids (chHCF101) of all photosynthetically active eukaryotes. Surprisingly, we found a second HCF101 paralog in all members of Cryptista, Haptista, and SAR that was predicted to predominantly target mitochondria (mHCF101), whereas Ind1 appeared to be absent in these organisms. We also identified a few exceptions, as apicomplexans possess mHCF101 predicted to localize in the cytosol and Nbp35 in the mitochondria. Our predictions were experimentally confirmed in selected representatives of Apicomplexa (Toxoplasma gondii), Stramenopila (Phaeodactylum tricornutum, Thalassiosira pseudonana), and Ciliophora (Tetrahymena thermophila) by tagging proteins with a transgenic reporter. Phylogenetic analysis suggested that chHCF101 and mHCF101 evolved from a common ancestral HCF101 independently of the Nbp35/Cfd1 and Ind1 proteins. Interestingly, phylogenetic analysis supports rather a lateral gene transfer of ancestral HCF101 from bacteria than its acquisition being associated with either α-proteobacterial or cyanobacterial endosymbionts. Conclusion Our searches for Nbp35-like proteins across eukaryotic lineages revealed that SAR, Haptista, and Cryptista possess mitochondrial HCF101. Because plastid localization of HCF101 was only known thus far, the discovery of its mitochondrial paralog explains confusion regarding the presence of HCF101 in organisms that possibly lost secondary plastids (e.g., ciliates, Cryptosporidium) or possess reduced nonphotosynthetic plastids (apicomplexans).

scholarly journals Overexpression of key sterol pathway enzymes in two model marine diatoms alters sterol profiles in Phaeodactylum tricornutum

2020 ◽  
Author(s):  
Ana Cristina Jaramillo-Madrid ◽  
Raffaela Abbriano ◽  
Justin Ashworth ◽  
Michele Fabris ◽  
Peter J. Ralph
Keyword(s):  
Intracellular Signaling ◽  
Phaeodactylum Tricornutum ◽  
Metabolic Flux ◽  
Total Sterol ◽  
Sterol Composition ◽  
Thalassiosira Pseudonana ◽  
Squalene Epoxidase ◽  
End Point ◽  
Eukaryotic Phytoplankton ◽  
Coa Reductase

AbstractSterols are a class of triterpenoid molecules with diverse functional roles in eukaryotic cells, including intracellular signaling and regulation of cell membrane fluidity. Diatoms are a dominant eukaryotic phytoplankton group that produce a wide diversity of sterol compounds. The enzymes 3-hydroxy-3-methyl glutaryl CoA reductase (HMGR) and squalene epoxidase (SQE) have been reported to be rate-limiting steps in sterol biosynthesis in other model eukaryotes; however, the extent to which these enzymes regulate triterpenoid production in diatoms is not known. To probe the role of these two metabolic nodes in the regulation of sterol metabolic flux in diatoms, we independently over-expressed two versions of the native HMGR and a conventional, heterologous SQE gene in the diatoms Thalassiosira pseudonana and Phaeodactylum tricornutum. Overexpression of these key enzymes resulted in significant differential accumulation of downstream sterol pathway intermediates in P. tricornutum. HMGR-mVenus overexpression resulted in the accumulation of squalene, cycloartenol, and obtusifoliol, while cycloartenol and obtusifoliol accumulated in response to heterologous NoSQE-mVenus overexpression. In addition, accumulation of the end-point sterol 24-methylenecholesta-5,24(24’)-dien-3β-ol was observed in all P. tricornutum overexpression lines, and campesterol increased 3-fold in P. tricornutum lines expressing NoSQE-mVenus. Minor differences in end-point sterol composition were also found in T. pseudonana, but no accumulation of sterol pathway intermediates was observed. Despite the successful manipulation of pathway intermediates and individual sterols in P. tricornutum, total sterol levels did not change significantly in transformed lines, suggesting the existence of tight pathway regulation to maintain total sterol content.

scholarly journals How marine diatoms cope with metal challenge: Insights from the morphotype-dependent metal tolerance in Phaeodactylum tricornutum

2021 ◽  
Vol 208 ◽  
pp. 111715
Author(s):  
Jie Ma ◽  
Beibei Zhou ◽  
Fengyuan Chen ◽  
Ke Pan
Keyword(s):  
Phaeodactylum Tricornutum ◽  
Metal Tolerance ◽  
Marine Diatoms
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