Current Proceedings on Technology

Yazarlar: Jahanbakhsh Godehkahriz Sodabeh, Alirezaee Kobra, Davar Robab

Konular:-

Anahtar Kelimeler:Assay,Progenesis,Software,Protein TerC & DanK

Özet: Proteomic approaches combining two-dimensional gel electrophoresis (2-DE), bioinformatics analysis and mass spectrometry were applied to identify stress-ralated proteins. This research was study proteomical analysis with Progenesis Software V.2.0 under vernalization cold. Leaf total protein extraction was carried out using IPG. The gels were analyzed by Progenesis software V.2.0. A match set was created from the protein patterns of four gels for each independent extract which allows spot matching among multiple gels. Proteins that showed changes in expression were identified by mass spectrometry using MS/QTOF. TerC and DnaK were two of the important proteins that showed the significant difference between two temperature treatments. DanK molecular chaperone plays an essential role in the folding of newly synthesized polypeptides and in the refolding of denatured proteins. DanK and it’scogenate proteins consist of a highly conserved NH2-terminal ATPase domain and a COOH-terminal peptide-binding domain. The TerC serves as a key component of the tellurite resistance operon in prokariotes, It’s function has remained undetermined until now. Nonetheiess, it is thought that the TerC protein may play one of the key roles in tellurite resistance mechanim it is thought that the TerCtellurite resistance C protein has a different function that the function of transmembrane transport postulated for TeO3-2.

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