Determinants of affinity and specificity in RNA-binding proteins.
Emerging data suggest that the mechanisms by which RNA-binding proteins (RBPs) interact with RNA and the rules governing specificity might be substantially more complex than those underlying their DNA-binding counterparts. Even our knowledge of what constitutes the RNA-bound proteome is contentious; recent studies suggest that 10-30% of RBPs contain no known RNA-binding domain. Adding to this situation is a growing disconnect between the avalanche of identified interactions between proteins and long noncoding RNAs and the absence of biophysical data on these interactions. RNA-protein interactions are also at the centre of what might emerge as one of the biggest shifts in thinking about cell and molecular biology this century, following from recent reports of ribonucleoprotein complexes that drive reversible membrane-free phase separation events within the cell. Unexpectedly, low-complexity motifs are important in the formation of these structures. Here we briefly survey recent advances in our understanding of the specificity of RBPs.
School of Life and Environmental Sciences, The University of Sydney, NSW 2006, Australia.
Stephanie
S
Helder
School of Chemistry and Biochemistry, The University of Western Australia, Crawley, WA 6014, Australia.
Amanda J
AJ
Blythe
School of Chemistry and Biochemistry, The University of Western Australia, Crawley, WA 6014, Australia.
Charles S
CS
Bond
School of Life and Environmental Sciences, The University of Sydney, NSW 2006, Australia. Electronic address: joel.mackay@sydney.edu.au.
Joel P
JP
Mackay
D006801:Humans; D011485:Protein Binding; D000072417:Protein Domains; D062085:RNA, Long Noncoding / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity
D062085:RNA, Long Noncoding; D016601:RNA-Binding Proteins