Protein dimers and multimers are often employed by nature for DNA and RNA handling and formation of specific, high-affinity protein-oligonucleotide complexes. The repeating structure of dsDNA lends itself to recognition by multimeric protein complexes that can assemble about the helical structure. In the cases of both DNA and RNA, specific recognition of nucleotide sequences can be achieved by multidomain proteins or protein multimers. Furthermore large multimeric assemblies are utilised for the stable formation of structures such as rings and filaments. Also, the assembly of multimeric structures by interchangeable subunits can add layers of regulation and increase functional complexity. Thus there appear to be many advantages to oligonucleotide interactions that are conferred by dimerisation or multimerisation.
|Title of host publication||Protein Dimerization and Oligomerization in Biology|
|Editors||J M Matthews|
|Place of Publication||USA|
|Pages||91 - 104|
|Number of pages||14|
|Publication status||Published - 2012|
Wilce, J. A., Vivian, J. P., & Wilce, M. C. (2012). Oligonucleotide binding proteins: the occurrence of dimer and multimer formation. In J. M. Matthews (Ed.), Protein Dimerization and Oligomerization in Biology (1st ed., pp. 91 - 104). Springer. https://doi.org/10.1007/978-1-4614-3229-6_6