ABSTRACT
Proteins and nucleic acids can bind in dierent ways. In general, it can be divided into the sequence-specic binding and non-sequence-specic binding [4,5]. e nucleic acid binding regions of proteins are always located in the conserved domains, where multiple DNA-or RNA-binding domains (DBDs or RBDs) are found within their tertiary structures. erefore, the identity of the individual domains and their relative arrangement are functionally important for the protein-nucleic acid binding. Several common DBDs have been discovered, including zinc nger [6], helix-turn-helix [7], helix-loop-helix [8], winged helix [9], and leucine zipper [10]. RNA-binding specicity and function are determined by the zinc nger [6], K homology [11], S1 [12], PAZ [13], PUF [14], PIWI [15], and RNA recognition motif (RRM) domains [16-18]. e binding anity can be further increased through protein oligomerization or multidomain protein complex.
