A low-temperature-responsive gene from barley encodes a protein with single-stranded nucleic acid-binding activity which is phosphorylated in vitro
| Autor: | Robert N. Lightowlers, Monica A. Hughes, Dunn Ma, Brown K |
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| Rok vydání: | 1996 |
| Předmět: |
DNA
Complementary Molecular Sequence Data DNA Single-Stranded Plant Science Biology chemistry.chemical_compound Genetics Amino Acid Sequence Phosphorylation Protein kinase A Peptide sequence Plant Proteins Messenger RNA Expression vector Base Sequence Sequence Homology Amino Acid RNA-Binding Proteins Hordeum General Medicine Blotting Northern Cyclic AMP-Dependent Protein Kinases Fusion protein Molecular biology DNA-Binding Proteins Biochemistry chemistry Nucleic acid Hordeum vulgare Agronomy and Crop Science DNA |
| Zdroj: | Plant Molecular Biology. 30:947-959 |
| ISSN: | 1573-5028 0167-4412 |
| Popis: | A low-temperature-responsive gene, blt 801, isolated from a winter barley (Hordeum vulgare L.) cDNA library prepared from leaf meristematic tissue, was sequenced. The deduced amino acid sequence predicts a glycine-rich RNA-binding protein (GR-RNP) which was homology to stress-responsive GR-RNPs from several other plant species. BLT 801 is a two-domain protein, the amino-terminal domain comprises a consensus RNA-binding domain similar to that found in many eukaryotic genes and the carboxy-terminal domain is extremely glycine-rich (68.5% glycine). Blt 801 mRNA also accumulates in response to the phytohormone abscisic acid. The protein encoded by blt 801 has been produced as a recombinant fusion protein using a bacterial expression vector. The fusion protein, a chimaera of glutathione S-transferase and BLT 801, has been used in studies to determine nucleic acid binding and other characteristics. Binding studies with single-stranded nucleic acids show that BLT 801 has affinity for homoribopolymers G, A and U but not C, it also binds to single-stranded DNA and selects RNA molecules containing open loop structures enriched in adenine but low in cytosine. Blt 801 has a consensus motif for phosphorylation by cAMP protein kinase (PKA) at the junction between the two domains which can be phosphorylated by PKA in vitro and which, by analogy to animal studies, may have significance for controlling enzyme function. |
| Databáze: | OpenAIRE |
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