Cold shock domain proteins and glycine-rich RNA-binding proteins from Arabidopsis thaliana can promote the cold adaptation process in Escherichia coli

• Published in: Nucleic acids research 2007-01, Vol.35 (2), p.506-516
• Main Authors: Kim, Jin Sun, Park, Su Jung, Kwak, Kyung Jin, Kim, Yeon Ok, Kim, Joo Yeol, Song, Jinkyung, Jang, Boseung, Jung, Che-Hun, Kang, Hunseung
• Format: Article
• Language: English
• Subjects: Acclimatization; Arabidopsis Proteins - genetics; Arabidopsis Proteins - metabolism; Arabidopsis Proteins - physiology; Arabidopsis thaliana; Cell Division; Cold Shock Proteins and Peptides; Cold Temperature; DNA-Binding Proteins - metabolism; DNA-Binding Proteins - physiology; Escherichia coli; Escherichia coli - genetics; Escherichia coli - growth & development; Gene Expression Regulation, Plant; Molecular Chaperones - genetics; Molecular Chaperones - metabolism; Molecular Chaperones - physiology; Nucleic Acid Conformation; RNA; RNA - chemistry; RNA - metabolism; RNA-Binding Proteins - genetics; RNA-Binding Proteins - metabolism; RNA-Binding Proteins - physiology
• ISSN: 0305-1048; 1362-4962
• DOI: 10.1093/nar/gkl1076

Despite the fact that cold shock domain proteins (CSDPs) and glycine-rich RNA-binding proteins (GRPs) have been implicated to play a role during the cold adaptation process, their importance and function in eukaryotes, including plants, are largely unknown. To understand the functional role of plant CSDPs and GRPs in the cold response, two CSDPs (CSDP1 and CSDP2) and three GRPs (GRP2, GRP4 and GRP7) from Arabidopsis thaliana were investigated. Heterologous expression of CSDP1 or GRP7 complemented the cold sensitivity of BX04 mutant Escherichia coli that lack four cold shock proteins (CSPs) and is highly sensitive to cold stress, and resulted in better survival rate than control cells during incubation at low temperature. In contrast, CSDP2 and GRP4 had very little ability. Selective evolution of ligand by exponential enrichment (SELEX) revealed that GRP7 does not recognize specific RNAs but binds preferentially to G-rich RNA sequences. CSDP1 and GRP7 had DNA melting activity, and enhanced RNase activity. In contrast, CSDP2 and GRP4 had no DNA melting activity and did not enhance RNAase activity. Together, these results indicate that CSDPs and GRPs help E.coli grow and survive better during cold shock, and strongly imply that CSDP1 and GRP7 exhibit RNA chaperone activity during the cold adaptation process.