Structure and function of a novel cold regulated cold shock domain containing protein from an obligate psychrophilic yeast, Glaciozyma antarctica
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...
| _version_ | 1796910673637146624 |
|---|---|
| author | Jennifer Charles Makdi Masnoddin Farhan Nazaie Nur Athirah Yusof |
| author_facet | Jennifer Charles Makdi Masnoddin Farhan Nazaie Nur Athirah Yusof |
| author_sort | Jennifer Charles |
| collection | UMS |
| description | 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. Recombinant protein expression of Ga16676 showed over expressed soluble expression in both supernatant and pellet forms at 20 . The effects of recombinant CSD ℃ protein overexpression on colony formation shows that E. coli cells were able to grow at 37 and 20 but not at 4 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 . 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. |
| first_indexed | 2024-03-06T03:07:46Z |
| format | Article |
| id | ums.eprints-27494 |
| institution | Universiti Malaysia Sabah |
| language | English English |
| last_indexed | 2024-03-06T03:07:46Z |
| publishDate | 2020 |
| publisher | Advances in Polar Science |
| record_format | dspace |
| spelling | ums.eprints-274942021-06-30T10:48:11Z https://eprints.ums.edu.my/id/eprint/27494/ Structure and function of a novel cold regulated cold shock domain containing protein from an obligate psychrophilic yeast, Glaciozyma antarctica Jennifer Charles Makdi Masnoddin Farhan Nazaie Nur Athirah Yusof QK Botany S Agriculture (General) 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. Recombinant protein expression of Ga16676 showed over expressed soluble expression in both supernatant and pellet forms at 20 . The effects of recombinant CSD ℃ protein overexpression on colony formation shows that E. coli cells were able to grow at 37 and 20 but not at 4 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 . 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. Advances in Polar Science 2020-06-30 Article PeerReviewed text en https://eprints.ums.edu.my/id/eprint/27494/1/Structure%20and%20function%20of%20a%20novel%20cold%20regulated%20cold%20shock%20domain%20containing%20protein%20from%20an%20obligate%20psychrophilic%20yeast%2C%20Glaciozyma%20antarctica-Abstract.pdf text en https://eprints.ums.edu.my/id/eprint/27494/2/Structure%20and%20function%20of%20a%20novel%20cold%20regulated%20cold%20shock%20domain%20containing%20protein%20from%20an%20obligate%20psychrophilic%20yeast%2C%20Glaciozyma%20antarctica.pdf 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. Advances in Polar Science, 31 (2). pp. 137-145. ISSN 1674-9928 http://www.aps-polar.org/paper/2020/31/02/A200512000004 10.13679/j.advps. 2019.0030 10.13679/j.advps. 2019.0030 |
| spellingShingle | QK Botany S Agriculture (General) Jennifer Charles Makdi Masnoddin Farhan Nazaie Nur Athirah Yusof Structure and function of a novel cold regulated cold shock domain containing protein from an obligate psychrophilic yeast, Glaciozyma antarctica |
| title | Structure and function of a novel cold regulated cold shock domain containing protein from an obligate psychrophilic yeast, Glaciozyma antarctica |
| title_full | Structure and function of a novel cold regulated cold shock domain containing protein from an obligate psychrophilic yeast, Glaciozyma antarctica |
| title_fullStr | Structure and function of a novel cold regulated cold shock domain containing protein from an obligate psychrophilic yeast, Glaciozyma antarctica |
| title_full_unstemmed | Structure and function of a novel cold regulated cold shock domain containing protein from an obligate psychrophilic yeast, Glaciozyma antarctica |
| title_short | Structure and function of a novel cold regulated cold shock domain containing protein from an obligate psychrophilic yeast, Glaciozyma antarctica |
| title_sort | structure and function of a novel cold regulated cold shock domain containing protein from an obligate psychrophilic yeast glaciozyma antarctica |
| topic | QK Botany S Agriculture (General) |
| url | https://eprints.ums.edu.my/id/eprint/27494/1/Structure%20and%20function%20of%20a%20novel%20cold%20regulated%20cold%20shock%20domain%20containing%20protein%20from%20an%20obligate%20psychrophilic%20yeast%2C%20Glaciozyma%20antarctica-Abstract.pdf https://eprints.ums.edu.my/id/eprint/27494/2/Structure%20and%20function%20of%20a%20novel%20cold%20regulated%20cold%20shock%20domain%20containing%20protein%20from%20an%20obligate%20psychrophilic%20yeast%2C%20Glaciozyma%20antarctica.pdf |
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