A low-temperature-responsive gene from barley encodes a protein with single-stranded nucleic acid-binding activity which is phosphorylated in vitro

Ma, Dunn; Brown, Katharine A Robson; Lightowlers, RN; Ma, Huiqin

doi:10.1007/bf00020806

Cited by 66 publications

(34 citation statements)

References 43 publications

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“…Coldinduced RNA-binding proteins have been reported in barley (55), Arabidopsis (56), Brassica napus (57), and leafy spurge (58). These proteins commonly contain RRM domains or a consensus sequence-type RNA binding domain, which is found in diverse proteins with RNA binding activities including U1 small nuclear ribonucleoprotein A (59), poly(A)-binding protein (60), and nucleolin (54).…”

Section: Discussionmentioning

confidence: 99%

A Cold-regulated Nucleic Acid-binding Protein of Winter Wheat Shares a Domain with Bacterial Cold Shock Proteins

Karlson

Nakaminami

Toyomasu

et al. 2002

Journal of Biological Chemistry

144

154

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The molecular mechanisms of cold acclimation are still largely unknown; however, it has been established that overwintering plants such as winter wheat increases freeze tolerance during cold treatments. In prokaryotes, cold shock proteins are induced by temperature downshifts and have been proposed to function as RNA chaperones. A wheat cDNA encoding a putative nucleic acid-binding protein, WCSP1, was isolated and found to be homologous to the predominant CspA of Escherichia coli. The putative WCSP1 protein contains a three-domain structure consisting of an N-terminal cold shock domain with two internal conserved consensus RNA binding domains and an internal glycine-rich region, which is interspersed with three C-terminal CX 2 CX 4 HX 4 C (CCHC) zinc fingers. Each domain has been described independently within several nucleotide-binding proteins. Northern and Western blot analyses showed that WCSP1 mRNA and protein levels steadily increased during cold acclimation, respectively. WCSP1 induction was cold-specific because neither abscisic acid treatment, drought, salinity, nor heat stress induced WCSP1 expression. Nucleotide binding assays determined that WCSP1 binds ssDNA, dsDNA, and RNA homopolymers. The capacity to bind dsDNA was nearly eliminated in a mutant protein lacking C-terminal zinc fingers. Structural and expression similarities to E. coli CspA suggest that WCSP1 may be involved in gene regulation during cold acclimation.

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Section: Discussionmentioning

confidence: 99%

A Cold-regulated Nucleic Acid-binding Protein of Winter Wheat Shares a Domain with Bacterial Cold Shock Proteins

Karlson

Nakaminami

Toyomasu

et al. 2002

Journal of Biological Chemistry

144

154

View full text Add to dashboard Cite

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“…Instead of an RRM domain they have a cold-shock domain with only the RNP-1 sequence (Sachetto-Martins et al, 2000). Some of these GRPs are known to have in vitro RNA binding activity (Ludevid et al, 1992;Hirose et al, 1993;Freire et al, 1995;Hanano et al, 1996;Dunn et al, 1996) and also bind single-stranded DNA (Hirose et al, 1993;Dunn et al, 1996) and are phosphorylated in vitro (Dunn et al, 1996) and in vivo (Freire et al, 1995). Deletion assays conducted with the RZ-1 protein have shown that the RNA-binding domain and the C-terminal glycine-rich region are essential for RNA-binding activity (Hanano et al, 1996).…”

Section: Sugarcane Ests Encoding Rna-binding Grpsmentioning

confidence: 99%

Classification, expression pattern and comparative analysis of sugarcane expressed sequences tags (ESTs) encoding glycine-rich proteins (GRPs)

et al. 2001

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Since the isolation of the first glycine-rich proteins (GRPs) in plants a wealth of new GRPs have been identified. The highly specific but diverse expression pattern of grp genes, taken together with the distinct sub-cellular localization of some GRP groups, clearly indicate that these proteins are involved in several independent physiological processes. Notwithstanding the absence of a clear definition of the role of GRPs in plant cells, studies conducted with these proteins have provided new and interesting insights into the molecular biology and cell biology of plants. Complexly regulated promoters and distinct mechanisms for the regulation of gene expression have been demonstrated and new protein targeting pathways, as well as the exportation of GRPs from different cell types have been discovered. These data show that GRPs can be useful as markers and/or models to understand distinct aspects of plant biology. In this paper, the structural and functional features of these proteins in sugarcane (Saccharum officinarum L.) are summarized. Since this is the first description of GRPs in sugarcane, special emphasis has been given to the expression pattern of these GRP genes by studying their abundance and prevalence in the different cDNA-libraries of the Sugarcane Expressed Sequence Tag (SUCEST) project . The comparison of sugarcane GRPs with GRPs from other species is also discussed.

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“…An increase in gene expression in response to environmental stresses such as cold, drought or wounding is one of the typical features of plant glycine-rich RNA-binding proteins (Alba and Pages 1998;Sachetto-Martins et al 2000). Ribohomopolymer-binding assays showed that glycine-rich RNA-binding proteins such as those from maize (MA16, Ludevid et al 1992), Nicotiana sylvestris (GRP-1b, Hirose et al 1993;RGP-3, Moriguchi et al 1997), and barley (BLT801, Dunn et al 1996) have high affinity for poly(G) and poly(U).…”

Section: Introductionmentioning

confidence: 99%

Gene expression and genetic mapping analyses of a perennial ryegrass glycine-rich RNA-binding protein gene suggest a role in cold adaptation

et al. 2006

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A perennial ryegrass cDNA clone encoding a putative glycine-rich RNA binding protein (LpGRP1) was isolated from a cDNA library constructed from crown tissues of cold-treated plants. The deduced polypeptide sequence consists of 107 amino acids with a single N-terminal RNA recognition motif (RRM) and a single C-terminal glycine-rich domain. The sequence showed extensive homology to glycine-rich RNA binding proteins previously identified in other plant species. LpGRP1-specific genomic DNA sequence was isolated by inverse PCR amplification. A single intron which shows conserved locations in plant genes was detected between the sequence motifs encoding RNP-1 and RNP-2 consensus protein domains. Significant increase in the mRNA level of LpGRP1 was detected in root, crown and leaf tissues during the treatment of plants at 4°C, through which freezing tolerance is attained. The increase in the mRNA level was prominent at least 2 hr after commencement of the cold treatment, and persisted for at least one week. Changes in mRNA level induced by cold treatment were more obvious than those due to treatments with abscisic acid (ABA) and drought. The LpGRP1 protein was found to localize in the nucleus in onion epidermal cells, suggesting that it may be involved in pre-mRNA processing. The LpGRP1 gene locus was mapped to linkage group 2. Possible roles for the LpGRP1 protein in adaptation to cold environments are discussed.

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A low-temperature-responsive gene from barley encodes a protein with single-stranded nucleic acid-binding activity which is phosphorylated in vitro

Cited by 66 publications

References 43 publications

A Cold-regulated Nucleic Acid-binding Protein of Winter Wheat Shares a Domain with Bacterial Cold Shock Proteins

A Cold-regulated Nucleic Acid-binding Protein of Winter Wheat Shares a Domain with Bacterial Cold Shock Proteins

Classification, expression pattern and comparative analysis of sugarcane expressed sequences tags (ESTs) encoding glycine-rich proteins (GRPs)

Gene expression and genetic mapping analyses of a perennial ryegrass glycine-rich RNA-binding protein gene suggest a role in cold adaptation

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