Characterization of a family of ice-active proteins from the Ryegrass, Lolium perenne
| Autor: | Craig J. Marshall, Jerome Demmer, Angela DeAth, Prestidge Ross L, Sofia Corrales, Selvanesan Luxmanan, Claire Hall, Steven Anthony Fish, Krishnanand D. Kumble, David A. Wharton, Clare Elton |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
Signal peptide
medicine.disease_cause Lolium perenne General Biochemistry Genetics and Molecular Biology Heating Antifreeze protein Antifreeze Proteins Freezing Lolium medicine Escherichia coli Plant Proteins chemistry.chemical_classification Expressed sequence tag Sequence Homology Amino Acid biology cDNA library Ice Osmolar Concentration General Medicine biology.organism_classification Recombinant Proteins Amino acid chemistry Biochemistry Crystallization General Agricultural and Biological Sciences |
| Zdroj: | Cryobiology. 57:263-268 |
| ISSN: | 0011-2240 |
| DOI: | 10.1016/j.cryobiol.2008.09.005 |
| Popis: | Five genes coding for ice-active proteins were identified from an expressed sequence tag database of Lolium perenne cDNA libraries. Each of the five genes were characterized by the presence of an N-terminal signal peptide, a region enriched in hydrophilic amino acids and a leucine-rich region in four of the five genes that is homologous with the receptor domain of receptor-like protein kinases of plants. The C-terminal region of all five genes contains sequence homologous with Lolium and Triticum ice-active proteins. Of the four ice-active proteins (IAP1, IAP2, IAP3 and IAP5) cloned, three could be expressed in Escherichia coli and recovered in a functional form in order to study their ice activity. All three ice-active proteins had recrystallization inhibition activity but showed no detectable antifreeze or ice nucleation activity at the concentration tested. IAP2 and IAP5 formed distinct hexagonal-shaped crystals in the nanolitre osmometer as compared to the weakly hexagonal crystals produced by IAP3. |
| Databáze: | OpenAIRE |
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