Profiling of nucleic acid binding on HuProt human proteome microarrays can reveal interactions with the largest collection of individual human proteins available on a single slide. Nucleic acid-protein interactions regulate many aspects of gene expression and thus cell physiology and pathology. DNA-protein interactions occur via a range of binding motifs present in transcription factors and nuclear receptors (e.g. DNA-binding domains, zinc fingers, leucine zippers) and histones and nonhistone proteins interacting with chromatin, all of which can influence gene expression. For RNA, hundreds of RNA binding proteins (RBPs) have now been identified which interact with mRNAs, noncoding RNAs, microRNAs etc. and are involved in post-transcriptional gene regulation including gene silencing by RNAi.
A wide range of nucleic acid binding proteins is represented on the HuProt array (see protein coverage). The method for studying protein - nucleic acid interactions on HuProt arrays resembles that for protein-protein interactions and can lead to identification of novel binding proteins, complementing other physical and genetic methods and contributing to understanding of the functional pathways of nucleic acid interactomes.
Similar to array-based protein-protein interaction screening, the purified nucleic acid of interest is either fluorescently labelled for direct detection on the array or alternatively, a biotinylated nucleic acid can be detected by secondary incubation with fluorophore-labelled streptavidin.
See here for HuProt references in protein DNA/RNA interactions