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

Abstract

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.

An RNA recognition motif-containing protein is required for plastid RNA editing in Arabidopsis and maize

“…2) (23). GR-RBPs have been shown to be involved in the plant's response to environmental stresses, particularly cold (45,46). However, little is known about the molecular function of either GR-RBPs or mRBPs.…”

Comparison of structure, function and regulation of plant cold shock domain proteins to bacterial and animal cold shock domain proteins

“…WCSP1 complements the cold sensitive phenotype of the quadruple Csp-deletion strain of E. coli (BX04), indicating that this protein can function as an RNA chaperone in vivo in a bacterial system (30). Expression studies revealed that some Arabidopsis CSP transcripts are also increased upon cold stress treatment, indicating a potential role in cold adaptation (19,31,32). Arabidopsis thaliana cold shock domain proteins (AtCSPs) promote cold adaptation in bacteria (31)(32)(33)(34).…”

“…Expression studies revealed that some Arabidopsis CSP transcripts are also increased upon cold stress treatment, indicating a potential role in cold adaptation (19,31,32). Arabidopsis thaliana cold shock domain proteins (AtCSPs) promote cold adaptation in bacteria (31)(32)(33)(34). Using functional approaches, AtCSPs were shown to play an important role under low temperature stress conditions in planta (33,34).…”

“…It is well known that plant CSPs can complement the cold-sensitive phenotype in the E. coli CSP quadruple deletion strain (BX04), suggesting that plant CSPs can also act as chaperones during cold stress (30,31). The sub-cellular localization of WCSP1 to the endoplasmic reticulum indirectly suggests that it may perform a role in translation (30).…”

“…The quadruple Csp deletion mutants of E. coli showed elongated and filamentous cells at 15 o C due to defects in cell septum formation (27,31). The expression of CspD is dramatically induced during stationary phase growth.…”