Functional and structural analyses of an expansin-like protein from the antarctic yeast Glaciozyma antarctica PI12 reveal strategies of nutrient scavenging in the sea ice environment

Nooraisyah Mohamad Nor, Noor Haza Fazlin Hashim, Doris Huai Xia Quay, Nor Muhammad Mahadi, Rosli Md Illias, Farah Diba Abu Bakar, Abdul Munir Abdul Murad

Research output: Contribution to journalArticle

Abstract

Genome data mining of the Antarctic yeast, Glaciozyma antarctica PI12 revealed an expansin-like protein encoding sequence (GaEXLX1). The GaEXLX1 protein is 24.8 kDa with a high alkaline pI of 9.81. Homology modeling of GaEXLX1 showed complete D1 and D2 domains of a conventional expansin. The protein exhibited 36% sequence similarity to Clavibacter michiganensis EXLX1 (PDB: 4JCW). Subsequently, a recombinant GaEXLX1 protein was produced using Escherichia coli expression system. Incubation with Avicel, filter paper and cotton fiber showed that the protein can disrupt the surface of crystalline and pure cellulose, suggesting a cell wall modification activity usually exhibited by expansin-like proteins. Binding assays displayed that GaEXLX1 can bind to polymeric substrates, including those postulated to be present in the sea ice ecosystem such as crab chitin and moss lichenan. GaEXLX1 may assist in the recognition and loosening of these substrates in the sea ice prior to hydrolysis by other extracellular enzymes. Similar loosening mechanism to classical expansin-like protein has been postulated for this psychrophilic protein based on several conserved residues of GaEXLX1 involved in binding interaction identified by docking analyses.

Original languageEnglish
Pages (from-to)231-241
Number of pages11
JournalInternational Journal of Biological Macromolecules
Volume144
DOIs
Publication statusPublished - 1 Feb 2020

Fingerprint

Ice Cover
Sea ice
Fungal Proteins
Scavenging
Yeast
Nutrients
Proteins
Food
Cellulose
Cotton Fiber
Bryophyta
Recombinant proteins
Chitin
Cotton fibers
Data Mining
Substrates
Protein
Antarctica
Recombinant Proteins
Ecosystems

Keywords

  • Expansin
  • Polysaccharide binding
  • Psychrophilic yeast

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Economics and Econometrics
  • Energy(all)

Cite this

Functional and structural analyses of an expansin-like protein from the antarctic yeast Glaciozyma antarctica PI12 reveal strategies of nutrient scavenging in the sea ice environment. / Mohamad Nor, Nooraisyah; Hashim, Noor Haza Fazlin; Quay, Doris Huai Xia; Mahadi, Nor Muhammad; Illias, Rosli Md; Abu Bakar, Farah Diba; Murad, Abdul Munir Abdul.

In: International Journal of Biological Macromolecules, Vol. 144, 01.02.2020, p. 231-241.

Research output: Contribution to journalArticle

Mohamad Nor, Nooraisyah ; Hashim, Noor Haza Fazlin ; Quay, Doris Huai Xia ; Mahadi, Nor Muhammad ; Illias, Rosli Md ; Abu Bakar, Farah Diba ; Murad, Abdul Munir Abdul. / Functional and structural analyses of an expansin-like protein from the antarctic yeast Glaciozyma antarctica PI12 reveal strategies of nutrient scavenging in the sea ice environment. In: International Journal of Biological Macromolecules. 2020 ; Vol. 144. pp. 231-241.
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abstract = "Genome data mining of the Antarctic yeast, Glaciozyma antarctica PI12 revealed an expansin-like protein encoding sequence (GaEXLX1). The GaEXLX1 protein is 24.8 kDa with a high alkaline pI of 9.81. Homology modeling of GaEXLX1 showed complete D1 and D2 domains of a conventional expansin. The protein exhibited 36{\%} sequence similarity to Clavibacter michiganensis EXLX1 (PDB: 4JCW). Subsequently, a recombinant GaEXLX1 protein was produced using Escherichia coli expression system. Incubation with Avicel, filter paper and cotton fiber showed that the protein can disrupt the surface of crystalline and pure cellulose, suggesting a cell wall modification activity usually exhibited by expansin-like proteins. Binding assays displayed that GaEXLX1 can bind to polymeric substrates, including those postulated to be present in the sea ice ecosystem such as crab chitin and moss lichenan. GaEXLX1 may assist in the recognition and loosening of these substrates in the sea ice prior to hydrolysis by other extracellular enzymes. Similar loosening mechanism to classical expansin-like protein has been postulated for this psychrophilic protein based on several conserved residues of GaEXLX1 involved in binding interaction identified by docking analyses.",
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