Difference between revisions of "Part:BBa K2959003"
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<partinfo>BBa_K2959003 short</partinfo>
 
<partinfo>BBa_K2959003 short</partinfo>
  
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PsDef1 is present in  Pinus sylvestris seeds, vegetative and generative organs. The defensin encodes a protein of 83 amino acids in length, whose first 33 amino acids correspond to the ‘N-terminal signal peptide, it also has eight highly conserved cysteines residues that are predicted to form four disulfide bonds C3–C49, C14–C34, C20–C43, and C24–C451, which stabilize its structure making it resistant to environmental changes. Its conformation consists in a cysteine-stabilized αβ-motif (CSαβ) with a prominent α-helix and a triple-stranded antiparallel β-sheet that is stabilized by the 4 disulfide bonds.
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PsDef1 is present in  <i>Pinus sylvestris</i> seeds, vegetative and generative organs. The defensin encodes a protein of 83 amino acids in length, whose first 33 amino acids correspond to the ‘N-terminal signal peptide, it also has eight highly conserved cysteines residues that are predicted to form four disulfide bonds C3–C49, C14–C34, C20–C43, and C24–C45<sup>1</sup>, which stabilize its structure making it resistant to environmental changes<sup>2</sup>. Its conformation consists in a cysteine-stabilized αβ-motif (CSαβ) with a prominent α-helix and a triple-stranded antiparallel β-sheet that is stabilized by the 4 disulfide bonds<sup>1</sup>.
  
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Endogenous PsDef1 causes morphological changes in fungi mycelium  when interacting with the sphingolipid membrane on fungal cell, disrupting the membrane integrity. Antifungal activity towards phytopathogenic fungi Botrytis cinerea, Fusarium oxysporum, Fusarium solani and Heterobasidion annosum, has been demonstrated in a previous investigation by Bulat et al. (2017) and antimicrobial activity in Gram-positive (Bacillus pumilus) and Gram-negative bacteria (Pectobacterium carotovorum, Pseudomonas fluorescens).
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Endogenous PsDef1 causes morphological changes in fungi mycelium  when interacting with the sphingolipid membrane on fungal cell, disrupting the membrane integrity. Antifungal activity towards phytopathogenic fungi <i>Botrytis cinerea</i>, <i>Fusarium oxysporum</i>, <i>Fusarium solani</i>, and <i>Heterobasidion annosum</i> has been demonstrated; as well as its antimicrobial activity against Gram-positive (<i>Bacillus pumilus</i>) and Gram-negative bacteria (<i>Pectobacterium carotovorum</i>, <i>Pseudomonas fluorescens</i>)<sup>1</sup>.
  
 
The part is designed to code for a fusion protein of PsDef1 with a polyhistidine tag (6x His-Tag) at its N-terminus for purification by immobilized metal affinity chromatography.
 
The part is designed to code for a fusion protein of PsDef1 with a polyhistidine tag (6x His-Tag) at its N-terminus for purification by immobilized metal affinity chromatography.
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<span class='h3bb'>Sequence and Features</span>
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===Sequence and Features===
 
<partinfo>BBa_K2959003 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K2959003 SequenceAndFeatures</partinfo>
  
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===References===
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1. Bulat I. Khairutdinov, Elena A. Ermakova, Yuri M. Yusy- povych, Elena K. Bessolicina, Nadezhda B. Tarasova, Yana Y. Toporkova, Valentina Kovaleva, Yuriy F. Zuev, Irina V. Nesmelova, NMR structure, conformational dynamics, and biological activity of PsDef1 defensin from Pinus sylvestris, BBA - Proteins and Proteomics (2017), doi:10.1016/j.bbapap.2017.05.012
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2. Kovalyova, V. A., Gout, I. T., Kyamova, R. G., Filonenko, V. V., & Gout, R. T. (2007). Molecular cloning and characterization of defensin 1 from Scots pine. Biopolymers and Cell,23(5), 398-404. Retrieved July 26, 2019
  
 
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Revision as of 23:27, 15 September 2019


Pinus sylvestris Defensin 1

PsDef1 is present in Pinus sylvestris seeds, vegetative and generative organs. The defensin encodes a protein of 83 amino acids in length, whose first 33 amino acids correspond to the ‘N-terminal signal peptide, it also has eight highly conserved cysteines residues that are predicted to form four disulfide bonds C3–C49, C14–C34, C20–C43, and C24–C451, which stabilize its structure making it resistant to environmental changes2. Its conformation consists in a cysteine-stabilized αβ-motif (CSαβ) with a prominent α-helix and a triple-stranded antiparallel β-sheet that is stabilized by the 4 disulfide bonds1. Endogenous PsDef1 causes morphological changes in fungi mycelium when interacting with the sphingolipid membrane on fungal cell, disrupting the membrane integrity. Antifungal activity towards phytopathogenic fungi Botrytis cinerea, Fusarium oxysporum, Fusarium solani, and Heterobasidion annosum has been demonstrated; as well as its antimicrobial activity against Gram-positive (Bacillus pumilus) and Gram-negative bacteria (Pectobacterium carotovorum, Pseudomonas fluorescens)1. The part is designed to code for a fusion protein of PsDef1 with a polyhistidine tag (6x His-Tag) at its N-terminus for purification by immobilized metal affinity chromatography.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]

References

1. Bulat I. Khairutdinov, Elena A. Ermakova, Yuri M. Yusy- povych, Elena K. Bessolicina, Nadezhda B. Tarasova, Yana Y. Toporkova, Valentina Kovaleva, Yuriy F. Zuev, Irina V. Nesmelova, NMR structure, conformational dynamics, and biological activity of PsDef1 defensin from Pinus sylvestris, BBA - Proteins and Proteomics (2017), doi:10.1016/j.bbapap.2017.05.012 2. Kovalyova, V. A., Gout, I. T., Kyamova, R. G., Filonenko, V. V., & Gout, R. T. (2007). Molecular cloning and characterization of defensin 1 from Scots pine. Biopolymers and Cell,23(5), 398-404. Retrieved July 26, 2019