ArticlePlant molecular biology1996
A low-temperature-responsive gene from barley encodes a protein with single-stranded nucleic acid-binding activity which is phosphorylated in vitro.
Article in Plant molecular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 70 citations in OpenAlex.
- Proteomic analysis of near-isogenic lines reveals key biomarkers on wheat chromosome 4B conferring drought tolerance.The plant genome · 2024Article
- Genome-wide identification, phylogenetic analysis, and expression profiling of glycine-rich RNA-binding protein (GRPs) genes in seeded and seedless grapes (Physiology and molecular biology of plants : an international journal of functional plant biology · 2021Article
- Genome-Wide Association Study RevealsFrontiers in genetics · 2021Article
- Overexpression of a novel salt stress-induced glycine-rich protein gene from alfalfa causes salt and ABA sensitivity in Arabidopsis.Plant cell reports · 2013Article
- Expression conservation within the circadian clock of a monocot: natural variation at barley Ppd-H1 affects circadian expression of flowering time genes, but not clock orthologs.BMC plant biology · 2012Article
- Functional conservation of cold shock domains in bacteria and higher plants.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Gene expression and genetic mapping analyses of a perennial ryegrass glycine-rich RNA-binding protein gene suggest a role in cold adaptation.Molecular genetics and genomics : MGG · 2006Article
- Plants in a cold climate.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2002Review
- Molecular characterization of nucleus-localized RNA-binding proteins from higher plants.Plant molecular biology · 2002Article
- Genome analysis: RNA recognition motif (RRM) and K homology (KH) domain RNA-binding proteins from the flowering plant Arabidopsis thaliana.Nucleic acids research · 2002Article
- High expression level of a gene coding for a chloroplastic amino acid selective channel protein is correlated to cold acclimation in cereals.Plant molecular biology · 1999Article
- Cloning and characterization of cold-regulated glycine-rich RNA-binding protein genes from leafy spurge (Euphorbia esula L.) and comparison to heterologous genomic clones.Plant molecular biology · 1998Article
- A glycine-rich RNA-binding protein gene is differentially expressed during acute hypersensitive response following Tobacco Mosaic Virus infection in tobacco.Plant molecular biology · 1998Article
- mRNA stability and localisation of the low-temperature-responsive barley gene family blt14.Plant molecular biology · 1997Article
- Chromosome regions and stress-related sequences involved in resistance to abiotic stress in Triticeae.Plant molecular biologyReview
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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