Biochemical properties of the smallest PDI like protein of Arabidopsis thaliana (Abstract/Poster in convegno)

Type
Label
  • Biochemical properties of the smallest PDI like protein of Arabidopsis thaliana (Abstract/Poster in convegno) (literal)
Anno
  • 2014-01-01T00:00:00+01:00 (literal)
Alternative label
  • William Remelli, Anna Paola Casazza, Aldo Grasso and Aldo Ceriotti (2014)
    Biochemical properties of the smallest PDI like protein of Arabidopsis thaliana
    in XVII ENPER Meeting, Roca Vecchia - Melendugno (Lecce), 8-11/09/2014
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • William Remelli, Anna Paola Casazza, Aldo Grasso and Aldo Ceriotti (literal)
Note
  • Poster (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Institute of Agricultural Biology and Biotechnology (IBBA), National Research Council (CNR), Via Bassini 15, 20133 Milano, Italy (literal)
Titolo
  • Biochemical properties of the smallest PDI like protein of Arabidopsis thaliana (literal)
Abstract
  • Protein disulfide isomerases (PDI) assist in vivo protein folding by helping newly translated polypeptide chains to form native disulfide bonds. PDI structure consists in two tandem repeats of thioredoxin domains, a-b-b-'a', in which a and a' domains are catalytically active. This enzyme is the founding member of a family of proteins that vary in length and domain arrangement, but share the common structural feature of having at least one domain with a thioredoxin-like fold (1). In A. thaliana there are at least 12 putative PDI-like enzymes (PDIL) (2). Among them AtPDIL 5-1 is the only single domain member. The human counterpart (HsERp18) has been biochemical characterized as an ER-resident disulfide oxidase (3). Here we present a preliminary biochemical characterization of AtPDIL 5-1. De novo in silico structural analysis suggests that AtPDIL 5-1 maintains the Rossman folding typical of thioredoxin-like proteins. In order to assess the in vitro activity of the protein, AtPDIL 5-1 was over-expressed in E. coli. For comparison we also produced a recombinant version of a canonical PDI (AtPDIL 1-1) and a truncated form of it, consisting only in the a domain (PDIa). The proteins were expressed and purified via Ni-affinity chromatography and tested for in vitro thioredoxin-like activities. When compared to the recombinant full length and truncated PDIs, AtPDIL 5-1 is significantly less active in both the reduction and the oxidation assay. These preliminary data suggest that HsERp18 and AtPDIL 5-1 does not share the same catalytic activity thus justifying further studies on the biochemical properties of this protein. (literal)
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