{'fraction_non_alphanumeric': 0.025796661608497723, 'fraction_numerical': 0.004552352048558422, 'mean_word_length': 4.739130434782608, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
SLIRP interacts with helicases to facilitate 2'- O-methylation of ribosomal RNA and to promote translation.

SLIRP is a versatile protein that can interact with stem-loop structure in RNA and with G quadruplex DNA. By using a quantitative proteomic experiment, we found that SLIRP interacts with the majority of the human helicase proteome. We also found that these interactions facilitate 2'- O-methylation of a number of nucleosides in rRNA and promote protein translation. Hence, we uncovered a novel function of SLIRP protein and offered novel mechanistic insights into its function as a RNA chaperone and into the regulation of 2'- O-methylation of rRNA.