ArticleProceedings of the National Academy of Sciences of the United States of America2006
Functional conservation of cold shock domains in bacteria and higher plants.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed, 180 citations in OpenAlex.
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- YBX1 regulates RNA polymerase III transcripts to prevent inflammation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- CISP, an Intrinsically Disordered Cold-Inducible Barley Protein, Functions as a Small RNA Chaperone.Plant direct · 2026Article
- Molecular Evolution of Paralogous Cold Shock Proteins in E. coli: A Study of Asymmetric Divergence and Protein Functional Networks.Molecular biotechnology · 2026Article
- Integrative physiological and transcriptomic analysis provides insights on the molecular basis of ABA-enhanced drought tolerance in pear (Pyrus betulaefolia).BMC plant biology · 2025Article
- Horizontally acquired CSP genes contribute to wheat adaptation and improvement.Nature plants · 2025Article
- Article
- Prokaryotic morphological features and maintenance activities governed by seasonal productivity conditions.FEMS microbiology ecology · 2024Article
- Genome-wide identification of cold shock proteins (CSPs) in sweet cherry (Prunus avium L.) and exploring the differential responses of PavCSP1 and PavCSP3 to low temperature and salt stress.Genes & genomics · 2024Article
- PbrCSP1, a pollen tube-specific cold shock domain protein, is essential for the growth and cold resistance of pear pollen tubes.Molecular breeding : new strategies in plant improvement · 2024Article
- From Stress Tolerance to Virulence: Recognizing the Roles of Csps in Pathogenicity and Food Contamination.Pathogens (Basel, Switzerland) · 2024Review
- Article
- c-di-GMP regulates activity of the PlzA RNA chaperone from the Lyme disease spirochete.Molecular microbiology · 2023Article
- Candidate Genes Associated with Abiotic Stress Response in Plants as Tools to Engineer Tolerance to Drought, Salinity and Extreme Temperatures in Wheat: An Overview.Plants (Basel, Switzerland) · 2022Review
- Molecular identification, characterization, and antagonistic activity profiling ofJournal of advanced veterinary and animal research · 2022Article
- Article
- An Apoplastic Defensin of Wheat Elicits the Production of Extracellular Polysaccharides in Snow Mold.Plants (Basel, Switzerland) · 2021Article
- Assessing nucleic acid binding activity of four dinoflagellate cold shock domain proteins from Symbiodinium kawagutii and Lingulodinium polyedra.BMC molecular and cell biology · 2021Article
- LeveragingFrontiers in microbiology · 2021Review
- Pleiotropic roles of cold shock proteins with special emphasis on unexplored cold shock protein member of Plasmodium falciparum.Malaria journal · 2020Review
5 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Escherichia coli, a family of cold shock proteins (CSPs) function as transcription antiterminators or translational enhancers at low temperature by destabilizing RNA secondary structure. A wheat nucleic acid-binding protein (WCSP1) was found to contain a cold shock domain (CSD) bearing high similarity to E. coli cold shock proteins. In the present study, a series of mutations were introduced into WCSP1, and its functionality was investigated by using in vivo and in vitro assays in the context of functional conservation with E. coli CSPs. Constitutive expression of WT WCSP1 in an E. coli cspA, cspB, cspE, cspG quadruple deletion mutant complemented its cold-sensitive phenotype, suggesting that WCSP1 shares a function with E. coli CSPs for cold adaptation. In addition, transcription antitermination activity was demonstrated for WCSP1 by using an E. coli strain that has a hairpin loop upstream of a chloramphenicol resistance gene. In vitro dsDNA melting assays clearly demonstrated that WCSP1 melts dsDNA, an activity that was positively correlated to the ability to bind ssDNA. When mutations were introduced at critical residues within the consensus RNA binding motifs (RNP1 and RNP2) of WCSP1, it failed to melt dsDNA. Studies with WCSP1-GFP fusion proteins documented patterns that are consistent with ER and nuclear localization. In vivo and in vitro functional analyses, coupled with subcellular localization data, suggest that WCSP1 may function as a RNA chaperone to destabilize secondary structure and is involved in the regulation of translation under low temperature.
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