Amino acid sequence of an extracellular, phosphate-starvation-induced ribonuclease from cultured tomato (Lycopersicon esculentum) cells
| Autor: | Konrad Glund, Henk J. Bak, Peter Terpstra, Jaap J. Beintema, Wolfgang Jost |
|---|---|
| Přispěvatelé: | Groningen Biomolecular Sciences and Biotechnology |
| Jazyk: | angličtina |
| Rok vydání: | 1991 |
| Předmět: |
EXPRESSION
RNase P Sequence analysis PROTEINS NUCLEASE Molecular Sequence Data ASPERGILLUS-SAITOI RHIZOPUS-NIVEUS Biochemistry Phosphates SELF-INCOMPATIBILITY GENE NICOTIANA-ALATA Endoribonucleases Vegetables 1-CYCLOHEXYL-3-(2-MORPHOLINYL-(4)-ETHYL)CARBODIIMIDE Trypsin Ribonuclease Amino Acid Sequence Peptide sequence Cells Cultured chemistry.chemical_classification PURIFICATION biology Endoplasmic reticulum Hydrolysis Protein primary structure food and beverages Amino acid S-tag chemistry Enzyme Induction biology.protein MAJOR RIBONUCLEASE Sequence Alignment |
| Zdroj: | European Journal of Biochemistry, 198(1), 1-6. Blackwell Publishing Ltd |
| ISSN: | 0014-2956 |
| Popis: | The primary structure of an intracellular ribonuclease (RNase LX) from cultured tomato (Lycopersicon esculentum) cells has been determined. Previous studies have shown that the protein is located inside the tomato cells but outside the vacuoles and that its synthesis is induced after depleting the cells for phosphate [Loffler, A., Abel, S., Jost, W., Beintema, J. J., Glund, K. (1992) Plant Physiol. 98, 1472-1478]. Sequence analysis was carried out by analysis of peptides isolated after enzymatic and chemical cleavage of the protein. RNase LX consists of 213 amino acids and has a molecular mass of 24300 Da and an isoelectric point of 5.33. The enzyme contains 10 half-cystines and there are no potential N-glycosylation sites detectable in the sequence. RNase LX, as compared to an extracellular tomato RNase (RNase LE), which is also phosphate regulated and the amino acid sequence of which was recently established [Jost, W., Bak, H., Glund, K., Terpstra, P. & Beintema, J. J. (1991) Eur. J. Biochem. 198, 1-6] has 60% of all amino acids identical and in identical positions, revealing a high degree of similarity between both proteins. In contrast to RNase LE, RNase LX has a C-terminal extension of nine amino acids. The C-terminal tetrapeptide HDEF may be a retention signal of the protein in the endoplasmic reticulum. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text