scholarly journals Molecular Characterization and Expression Analysis of Toll-like Receptor 9 Gene in Turbot, Scophthalmus Maximus

2020 ◽  
Vol 1 (2) ◽  
Author(s):  
Guanjie Wang ◽  
Xuepeng Li ◽  
Qiuming Liu ◽  
Xianzhi Dong ◽  
Guobin Hu
Keyword(s):  
Interleukin 1 ◽  
Head Kidney ◽  
Scophthalmus Maximus ◽  
Peptide Sequence ◽  
Amino Acid Residues ◽  
Signal Peptide Sequence ◽  
Repeat Domain ◽  
Turbot Scophthalmus Maximus ◽  
Leucine Rich Repeats ◽  
Molecular Patterns

Toll-like receptors (TLRs) have emerged as key sensors of invading microbes by recognizing pathogen-associated molecular patterns and activating innate immune responses. TLR9 functions as a pattern-recognition receptor that recognizes unmethylated CpG motifs in bacterial and viral DNA. In this study, the full cDNA and genomic sequences of tlr9 in Scophthalmus maximus (smtlr9) were identified and characterized. The full-length cDNA of smtlr9 was of 3754 bp encoding a polypeptide of 1066 amino acid residues. The genome sequence of smtlr9 was composed of 4083 nucleotides, including three exons and two introns. The putative Smtlr9 protein was characterized by a signal peptide sequence, a leucine-rich repeat domain (LRD) containing 15 leucine-rich repeats (LRRs), a transmembrane region, and a Toll/interleukin-1 receptor (TIR) domain. The putative protein shows the highest sequence identity (36.0~73.6%) to human and fish TLR9s. Phylogenetic analysis grouped Smtlr9 with other teleost Tlr9s. The smtlr9 mRNA was constitutively expressed in all tissues examined, with the highest level in the head kidney and kidney. The smtlr9 transcription level was up-regulated by ODN2395 in the muscle, head kidney, spleen, and gills.

Different impact of heat-inactivated and viable lactic acid bacteria of aquatic origin on turbot (Scophthalmus maximus L.) head-kidney leucocytes

2015 ◽  
Vol 44 (1) ◽  
pp. 214-223 ◽  
Author(s):  
Estefanía Muñoz-Atienza ◽  
Carlos Araújo ◽  
Nuria Lluch ◽  
Pablo E. Hernández ◽  
Carmen Herranz ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Lactic Acid Bacteria ◽  
Head Kidney ◽  
Scophthalmus Maximus ◽  
Turbot Scophthalmus Maximus

Hemolysis of turbot(Scophthalmus maximus)blood cell with Quillaja saponaria saponin

2013 ◽  
Vol 37 (7) ◽  
pp. 1073
Author(s):  
Yujuan WANG ◽  
Xiuhua WANG ◽  
Wen HAN ◽  
Rui WANG ◽  
Jie HUANG
Keyword(s):  
Blood Cell ◽  
Scophthalmus Maximus ◽  
Quillaja Saponaria ◽  
Turbot Scophthalmus Maximus

scholarly journals Subcellular localization and purification of a p-hydroxyphenylpyruvate dioxygenase from cultured carrot cells and characterization of the corresponding cDNA

1997 ◽  
Vol 325 (3) ◽  
pp. 761-769 ◽  
Author(s):  
Isabelle GARCIA ◽  
Matthew RODGERS ◽  
Catherine LENNE ◽  
Anne ROLLAND ◽  
Alain SAILLAND ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Gel Filtration ◽  
Peptide Sequence ◽  
Amino Acid Residues ◽  
Carrot Cells ◽  
Expression Studies ◽  
Sds Page ◽  
Molecular Masses ◽  
The Difference ◽  
Dioxygenase Activity

p-Hydroxyphenylpyruvate dioxygenase catalyses the transformation of p-hydroxyphenylpyruvate into homogentisate. In plants this enzyme has a crucial role because homogentisate is the aromatic precursor of all prenylquinones. Furthermore this enzyme was recently identified as the molecular target for new families of potent herbicides. In this study we examine precisely the localization of p-hydroxyphenylpyruvate dioxygenase activity within carrot cells. Our results provide evidence that, in cultured carrot cells, p-hydroxyphenylpyruvate dioxygenase is associated with the cytosol. Purification and SDS/PAGE analysis of this enzyme revealed that its activity is associated with a polypeptide of 45–46 kDa. This protein specifically cross-reacts with an antiserum raised against the p-hydroxyphenylpyruvate dioxygenase of Pseudomonas fluorescens. Gel-filtration chromatography indicates that the enzyme behaves as a homodimer. We also report the isolation and nucleotide sequence of a cDNA encoding a carrot p-hydroxyphenylpyruvate dioxygenase. The nucleotide sequence (1684 bp) encodes a protein of 442 amino acid residues with a molecular mass of 48094 Da and shows specific C-terminal regions of similarity with other p-hydroxyphenylpyruvate dioxygenases. This cDNA encodes a functional p-hydroxyphenylpyruvate dioxygenase, as evidenced by expression studies with transformed Escherichia coli cells. Comparison of the N-terminal sequence of the 45–46 kDa polypeptide purified from carrot cells with the deduced peptide sequence of the cDNA confirms that this polypeptide supports p-hydroxyphenylpyruvate dioxygenase activity. Immunodetection studies of the native enzyme in carrot cellular extracts reveal that N-terminal proteolysis occurs during the process of purification. This proteolysis explains the difference in molecular masses between the purified protein and the deduced polypeptide.

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