Jennifer Charles and Makdi Masnoddin and Farhan Nazaie and Nur Athirah Yusof (2020) Structure and Function of a Novel Cold Regulated Cold Shock Domain Containing Protein from an Obligate Psychrophilic Yeast, Glaciozyma antarctica. Advance in Polar Science, 31 (2). ISSN 1674-9928
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Structure and Function of a Novel Cold Regulated Cold Shock Domain Containing Protein from an Obligate Psychrophilic Yeast, Glaciozyma antarctica.pdf Download (48kB) | Preview |
Abstract
Cold shock domain (CSD)-containing proteins are one of the groups of the evolutionarily conserved nucleic acid-binding proteins in all three domains of life consisting of an ancient beta-barrel fold that serves to bind nucleic acids. The cDNA of a novel protein-coding gene containing CSD was cloned from Glaciozyma antarctica designated as Ga16676. The full length of Ga16676 gene with the size of 1335 bp encodes for an N-terminal CSD with conserved nucleic acids binding motif RNP1 and RNP2. The Ga16676 gene was cloned in pET30 Ek/LIC, sequenced, expressed and its resistance towards cold was characterized. Protein expression of recombinant Ga16676 showed overexpressed soluble expression in both supernatant and pellet forms at 20°C. The effects of CSD protein overexpression on colony formation shows that E. coli cells were able to grow at 37°C and 20°C but not at 4°C while E. coli_Ga16676 cells were able to grow at all temperatures tested. In addition, E. coli_Ga16676 cells showed higher growth rate compared to empty E. coli cells at 10°C. Structural analysis of Ga16676 reveals some interesting findings such as more aromatic interactions for efficient binding in low energy environment, a longer loop that may contribute to structural flexibility and clustering of charged amino acids on the protein surface that is important for protein stability and flexibility.
| Item Type: | Article |
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| Keyword: | Cold shock protein, CSP, cold adaptation, cold stress, stress response, stress tolerance, Glaciozyma antarctica, psychrophilic yeast |
| Subjects: | Q Science > Q Science (General) |
| Department: | INSTITUTE > Biotechnology Research Institute (BRI) |
| Depositing User: | SITI AZIZAH BINTI IDRIS - |
| Date Deposited: | 21 Sep 2020 08:10 |
| Last Modified: | 21 Sep 2020 08:10 |
| URI: | https://eprints.ums.edu.my/id/eprint/25962 |
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