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Characterization of the Brassica rapa auxin amido-hydrolase, BrILL2


Savić, Bojana; Ludwig-Müller, Jutta; Tomić, Sanja; Magnus, Volker; Salopek-Sondi, Branka
Characterization of the Brassica rapa auxin amido-hydrolase, BrILL2 // Physiologia Plantarum, Special Issue, 133 (3) / Vaughan, Hurry (ur.).
Oxford: Blackwell Publishing, 2008. str. P01-065 (poster, međunarodna recenzija, sažetak, znanstveni)


Naslov
Characterization of the Brassica rapa auxin amido-hydrolase, BrILL2

Autori
Savić, Bojana ; Ludwig-Müller, Jutta ; Tomić, Sanja ; Magnus, Volker ; Salopek-Sondi, Branka

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Physiologia Plantarum, Special Issue, 133 (3) / Vaughan, Hurry - Oxford : Blackwell Publishing, 2008, P01-065

Skup
XVI Congress of the Federation of European Societies of Plant Biology (FESPB)

Mjesto i datum
Tampere, Finska, 17.8.-22.8.2008

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
Auxin amido-hydrolase; BrILL2; Brassica rapa; Amino acid conjugates; Enzymatic activity

Sažetak
Reversible conjugation with amino acids is used by plants to adjust endogenous auxin levels as required for concerted growth and development. One of the auxin-amidohydrolases included in this regulatory mechanism, BrILL2, was cloned from Chinese cabbage (Brassica rapa L.) and tested for hydrolytic activity towards conjugates of indole-3-acetic acid. We further characterized the enzyme including substrates such as alanine (Ala) conjugates of indole-3-propionic acid (IPA) and indole-3-butyric acid (IBA), both of which are endogenous auxins. Enzymatic activity of purified BrILL2 was tested in the presence of dithiothreitol and Mn++. Progress of the cleavage reaction was monitored by HPLC using absorbance at 284 nm. IPA-ala was hydrolyzed at the highest rate, followed by IBA-ala and IAA-ala, in this order. The 3D structure of Br-ILL2 was modeled by the program Modeller9v2 using the X-ray structure of IAA-aminoacid hydrolase from Arabidopsis thaliana (PDB_id 1XMB) and the Mn++ binding site was determined. Ligands: IBA-Ala, IPA-ala, IAA-Ala and IPA-Asp were docked into the protein using the AutoDock3.05 program. The most populated binding site was selected as the most probable one. The obtain complexes were neutralized by adding Na+ ions, the systems was solvated in the 8 Å ; ; thick water layer and energy minimized using the program AMBER9. To learn more about the complex stability and the substrate binding site we accomplished a series of molecular dynamics simulations.

Izvorni jezik
Engleski

Znanstvena područja
Fizika, Biologija



POVEZANOST RADA


Projekt / tema
098-0982913-2829 - Molekularna regulacija biljnog razvitka (Branka Salopek-Sondi, )
098-1191344-2860 - Proučavanje biomakromolekula računalnim metodama i razvoj novih algoritama (Sanja Tomić, )

Ustanove
Institut "Ruđer Bošković", Zagreb

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE