Abstract
In response to cold, E.coli accumulates a family of cold shock proteins (CSPs) that function as a RNA chaperone. Plant cold shock domain (CSD) proteins contain a CSD that is highly conserved with bacterial CSPs. Here, we performed functional characterization of one of the four Arabidopsis CSD proteins (AtCSP1). AtCSP1 mRNA was detectable at ambient temperature but was up-regulated in response to cold. We examined nucleic acid melting activity of AtCSP1 to determine the function of AtCSP1 as a RNA chaperone. AtCSP1 showed melting activity against double-stranded DNA. AtCSP1-promoter::GUS transgenic plants revealed tissue specific expression of AtCSP1 in shoots and root tips of seedling. Analysis of subcellular localization of a AtCSP1::GFP fusion protein detected signals within the nucleus and nucleolus in Arabidopsis root cells. These results suggested that AtCSP1 may be involved in nuclear RNA-processing events that are associated with regulation of developmental processes.
