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

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

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

1 Citation (Scopus)

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 publicationAIP Conference Proceedings
Pages292-297
Number of pages6
Volume1571
DOIs
Publication statusPublished - 2013
Event2013 UKM Faculty of Science and Technology Post-Graduate Colloquium - Selangor
Duration: 3 Jul 20134 Jul 2013

Other

Other2013 UKM Faculty of Science and Technology Post-Graduate Colloquium
CitySelangor
Period3/7/134/7/13

Fingerprint

Antarctic regions
crystallization
proteins
yeast
heat
shock
uniqueness
inserts
research and development
organisms
platforms
industries
costs

Keywords

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

ASJC Scopus subject areas

  • Physics and Astronomy(all)

Cite this

Cloning, expression and crystallisation of SGT1 Co-chaperone protein from Glaciozyma antarctica. / Yusof, Nur Athirah; Abu Bakar, Farah Diba; Beddoe, Travis; Abd. Murad, Abdul Munir.

AIP Conference Proceedings. Vol. 1571 2013. p. 292-297.

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

Yusof, NA, Abu Bakar, FD, Beddoe, T & Abd. Murad, AM 2013, Cloning, expression and crystallisation of SGT1 Co-chaperone protein from Glaciozyma antarctica. in AIP Conference Proceedings. vol. 1571, pp. 292-297, 2013 UKM Faculty of Science and Technology Post-Graduate Colloquium, Selangor, 3/7/13. https://doi.org/10.1063/1.4858671
@inproceedings{cd00a8b58d594a378967ca81b97a270e,
title = "Cloning, expression and crystallisation of SGT1 Co-chaperone protein from Glaciozyma antarctica",
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.",
keywords = "Cloning, Crystallization, Expression, HSP90, Molecular chaperone, SGT1",
author = "Yusof, {Nur Athirah} and {Abu Bakar}, {Farah Diba} and Travis Beddoe and {Abd. Murad}, {Abdul Munir}",
year = "2013",
doi = "10.1063/1.4858671",
language = "English",
isbn = "9780735411999",
volume = "1571",
pages = "292--297",
booktitle = "AIP Conference Proceedings",

}

TY - GEN

T1 - Cloning, expression and crystallisation of SGT1 Co-chaperone protein from Glaciozyma antarctica

AU - Yusof, Nur Athirah

AU - Abu Bakar, Farah Diba

AU - Beddoe, Travis

AU - Abd. Murad, Abdul Munir

PY - 2013

Y1 - 2013

N2 - 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.

AB - 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.

KW - Cloning

KW - Crystallization

KW - Expression

KW - HSP90

KW - Molecular chaperone

KW - SGT1

UR - http://www.scopus.com/inward/record.url?scp=84897778858&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84897778858&partnerID=8YFLogxK

U2 - 10.1063/1.4858671

DO - 10.1063/1.4858671

M3 - Conference contribution

SN - 9780735411999

VL - 1571

SP - 292

EP - 297

BT - AIP Conference Proceedings

ER -