| 1995 |
ROK1 encodes an essential yeast protein containing conserved DEAD-box domains characteristic of ATP-dependent RNA helicases; it was identified as a high-copy suppressor of the kem1 null mutation. |
Sequence analysis, genetic suppressor screen, viability assays |
Gene |
Medium |
8529880
|
| 1998 |
Rok1 protein (~64 kDa) is localized predominantly to the cytoplasm in vegetatively growing Saccharomyces cerevisiae cells, as determined by indirect immunofluorescence with affinity-purified anti-Rok1 antibodies. |
Western blot, indirect immunofluorescence |
Molecules and cells |
Medium |
9571634
|
| 1999 |
Rok1 possesses intrinsic ATPase activity, and mutations in conserved ATPase motifs abolish this activity and cause in vivo lethality, demonstrating that ATP hydrolysis is essential for Rok1 function. Notably, the ATPase activity is RNA-independent. |
In vitro ATPase assay with purified MBP-Rok1 fusion protein, site-directed mutagenesis, in vivo lethality tests |
Nucleic acids research |
High |
10373593
|
| 2008 |
The DEAD-box helicase Rok1 is specifically required for release of the essential snoRNA snR30 from pre-ribosomes during 40S subunit synthesis. Point mutations in helicase motif I impair snR30 release, while motif III mutations do not, indicating mechanistic specificity of different helicase motifs. |
Quantitative snoRNA association screen (Northern blot-based), helicase domain point mutations, yeast depletion strains |
EMBO reports |
High |
18833290
|
| 2010 |
Rok1 protein levels oscillate during the yeast cell cycle (declining at G1/S, increasing at G2), controlled by two upstream open reading frames (uORFs) in the ROK1 5'-UTR that inhibit translation. Disrupting uORFs elevates Rok1 levels and causes delays in bud emergence and recovery from pheromone arrest. |
uORF mutagenesis, Western blot cell-cycle analysis, pheromone arrest/release assays |
FEBS letters |
Medium |
20969870
|
| 2014 |
UV cross-linking (CRAC) revealed that Rok1 directly contacts pre-rRNA at multiple sites clustering in the 'foot' region of the small ribosomal subunit, particularly the expansion segment ES6, where it promotes snR30 release. CLASH further identified novel pre-rRNA base-pairing sites for snR30, snR10, U3, and U14 clustering in expansion segments, suggesting these snoRNAs bridge long-range rRNA interactions during early ribosome assembly. |
UV cross-linking and analysis of cDNA (CRAC), cross-linking ligation and sequencing of hybrids (CLASH) |
RNA (New York, N.Y.) |
High |
24947498
|
| 2015 |
Three ROK1 5'-UTR-binding proteins—Psk2 (PAS kinase), Skp1, and Tub4—regulate Rok1 translation through uORF1: Psk2 and Skp1 repress Rok1 synthesis, while Tub4 promotes it, acting downstream of uORF1-mediated inhibition. |
Yeast three-hybrid screening, PSK2 deletion analysis, temperature-sensitive alleles of SKP1 and TUB4 |
Journal of microbiology (Seoul, Korea) |
Medium |
26310304
|
| 2016 |
ATP-bound (but not ADP-bound) Rok1 stabilizes Rrp5 binding to pre-40S ribosomes, and ATP hydrolysis by Rok1 is required to release Rrp5 from pre-40S ribosomes in vivo, freeing Rrp5 to participate in 60S subunit assembly. Blocked Rrp5 release causes secondary accumulation of snR30. An interaction between Rrp5 and the DEAD-box protein Has1 is implicated in snR30 accumulation when Rrp5 release is blocked. |
In vivo and in vitro biochemical analyses, ATP/ADP-form Rok1 binding assays, Rrp5 co-immunoprecipitation, functional epistasis |
PLoS biology |
High |
27280440
|
| 2021 |
Ddx52 (the zebrafish ortholog of DDX52) maintains the level of 47S precursor ribosomal RNA and is essential for juvenile growth; loss-of-function by temperature-sensitive mutation suspends whole-organism growth reversibly. |
Forward genetic screen, positional cloning, complementation assays, 47S pre-rRNA quantification |
Development (Cambridge, England) |
Medium |
34323273
|
| 2021 |
DDX52 knockdown in prostate cancer cells inhibits cell growth in vitro and in vivo, and suppresses c-Myc signaling; conversely, c-Myc transcriptionally regulates DDX52 expression, forming a positive feedback loop. |
shRNA knockdown, RNA sequencing, GSEA, Western blot, xenograft mouse model, IHC |
Cancer cell international |
Low |
34399732
|
| 2021 |
DDX52 knockdown suppresses melanoma cell proliferation and tumor growth, and an RNA immunoprecipitation assay confirmed physical association between DDX52 protein and c-Myc mRNA; restoration of c-Myc partly rescues DDX52-deficiency phenotypes. |
shRNA knockdown, RNA immunoprecipitation (RIP), xenograft mouse model, rescue assay |
Bioengineered |
Medium |
34233596
|
| 2022 |
In Drosophila, Rok1 and its cofactor Rrp5 co-localize to the nucleolus and are both required for pre-rRNA processing and ribosome assembly. Loss of Rok1 causes nucleolar enlargement, stalled ribosome assembly, and inhibition of mitosis in the brain. Rok1 depletion also mislocalizes Rrp5 within the nucleolus, suggesting Rok1 is required for accurate Rrp5 positioning. |
Genetics (mutant analysis), fluorescence in situ hybridization (FISH), developmental phenotype assays |
International journal of molecular sciences |
Medium |
35628496
|
| 2026 |
Human DDX52 is an ATP-dependent 3'-to-5' translocase/helicase that can unwind DNA duplexes and DNA/RNA hybrids in vitro. DDX52 also functions as a nucleic acid annealase (strand annealing), an activity that requires the N-terminal intrinsically disordered region (IDR) and becomes hyperactive when helicase activity is abolished by mutagenesis. CRISPR-generated DDX52+/- U2OS cells exhibit growth defects and impaired cell migration. |
In vitro helicase/translocase assay, strand-annealing assay, helicase-dead mutagenesis, CRISPR-Cas9 heterozygous knockout, cell migration assay |
Bioscience reports |
High |
41510705
|
| 2026 |
In fission yeast, rok1 deletion shortens and slows actin ring contraction during cytokinesis and inhibits kinetochore separation during mitosis. Transcriptomic analysis identified upregulation of myo51 and blt1 (delaying actin ring assembly) and psm3/psc3 cohesin subunits as key downstream effectors of Rok1 deletion phenotypes. |
Fluorescent protein labeling, live-cell imaging, RNA sequencing, bioinformatics |
Experimental and therapeutic medicine |
Low |
42016605
|