Cloning, expression and crystallisation of SGT1 Co-chaperone protein from Glaciozyma antarctica

Nur Athirah Yusof, Farah Diba Abu Bakar, Travis Beddoe, Abdul Munir Abdul Murad

Research output: Chapter in Book/Report/Conference proceedingConference PaperResearch

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Abstract

Studies on psycrophiles are now in the limelight of todays post genomic era as they fascinate the research and development industries. The discovery from Glaciozyma antarctica, an extreme cold adapted yeast from Antarctica shows promising future to provide cost effective natural sustainable energy and create wider understanding of the property that permits this organisms to adapt to extreme temperature downshift. In plants and yeast, studies show the interaction between SGT1 and HSP90 are essential for disease resistance and heat stress by activating a number of resistance proteins. Here we report for the first time cloning, expression and crystallization of the recombinant SGT1 protein of G. antarctica (rGa-SGT1), a highly conserved eukaryotic protein that interacts with the molecular chaperones HSP90 (heat shock protein 90) apparently associated in a role of co-chaperone that may play important role in cold adaptation. The sequence analysis of rGa-SGT1 revealed the presence of all the characteristic features of SGT1 protein. In this study, we present the outlines and results of protein structural study of G. antarctica SGT1 protein. We validate this approach by starting with cloning the target insert into Ligation Independent Cloning system proceeded with expression using E. coli system, and crystallisation of the target rGA-SGT1 protein. The work is still on going with the target subunit of the complex proteins yielded crystals. These results, still ongoing, open a platform for better understanding of the uniqueness of this crucial molecular machine function in cold adaptation.

Original languageEnglish
Title of host publication2013 UKM FST Postgraduate Colloquium - Proceedings of the Universiti Kebangsaan Malaysia, Faculty of Science and Technology 2013 Postgraduate Colloquium
Pages292-297
Number of pages6
Volume1571
DOIs
Publication statusPublished - 2013
EventUniversiti Kebangsaan Malaysia Faculty of Science and Technology Post-Graduate Colloquium 2013 - Selangor, Malaysia
Duration: 3 Jul 20134 Jul 2013

Conference

ConferenceUniversiti Kebangsaan Malaysia Faculty of Science and Technology Post-Graduate Colloquium 2013
CountryMalaysia
CitySelangor
Period3/07/134/07/13

Keywords

  • Cloning
  • Crystallization
  • Expression
  • HSP90
  • Molecular chaperone
  • SGT1

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