Cold Shock Domain Proteins in Arabidopsis: Functions in Stress Tolerance and Development
Cold shock domain (CSD) is a highly conserved nucleic acid-binding domain that is found from bacteria to human. Bacterial CSD proteins (or cold shock proteins) destabilize RNA secondary structures and regulate transcription and translation. This function, referred to RNA chaperone, is essential for bacterial cold adaptation. In eukaryotes, CSDs are found as a functional domain of multidomain proteins. Lin28 is one of the animal CSD proteins that is associated with cell pluripotency. Lin28 has one CSD and two copies of Cys-Cys-His-Cys (CCHC) zinc fingers and binds pri-let-7 miRNA to protect it from microprocessing. Plant CSD proteins commonly contain a CSD and several copies of CCHC zinc fingers. Arabidopsis has four CSD proteins and their functions have been extensively studied recently. In this chapter, we review current status of the researches on the functions of plant CSD proteins using Arabidopsis as a model.
KeywordsZinc Bacillus Dehydration Editing Gibberellin
- Kim M-H, Sonoda Y, Sasaki K, Kaminaka H, Imai R (2013) Interactome analysis reveals versatile functions of Arabidopsis COLD SHOCK DOMAIN PROTEIN 3 in RNA processing within the nucleus and cytoplasm. Cell Stress Chaperones.18:517–525Google Scholar
- Mitchell SA, Spriggs KA, Coldwell MJ, Jackson RJ (2003) The Apaf-1 internal ribosome entry segment attains the correct structural conformation for function via interactions with PTB and unr. Mol Cell 11:757–771Google Scholar