Ask about this productRelated genes to: DHX29 antibody
- Gene:
- DHX29 NIH gene
- Name:
- DExH-box helicase 29
- Previous symbol:
- DDX29
- Synonyms:
- -
- Chromosome:
- 5q11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2001-07-18
- Date modifiied:
- 2016-09-27
Related products to: DHX29 antibody
Related articles to: DHX29 antibody
- The genetic code determines not only the amino acid sequences of proteins but also mRNA stability. How is this hidden message read? Hia and colleagues have now identified human DHX29 as a reader of the mRNA stability code carried by codons, providing new mechanistic insights into translation-coupled gene regulation. - Source: PubMed
Publication date: 2026/07/06
Mishima Yuichiro - The DEAD-box helicase DHX29 plays a critical role in the translation of mRNAs containing complex RNA secondary structure in their 5' untranslated regions (UTRs). The human cytomegalovirus (HCMV) genome has a high GC content, suggesting that the 5' UTRs of viral mRNAs may contain significant secondary structure and require DHX29 for efficient translation. We found that depleting DHX29 from primary human fibroblasts prior to infection reduced viral mRNA and protein levels and decreased HCMV replication. The defect in HCMV replication correlated with decreased expression of the HCMV immediate-early proteins IE1 and IE2, which are necessary for the establishment of lytic infection. Analysis of polysome-associated mRNAs revealed that the defect in IE1 and IE2 expression is due to decreased mRNA translation efficiency. DHX29 depletion led to reduced levels of the eIF4F translation initiation complex, resulting from decreased translation of the eIF4G1 mRNA. However, in line with our previous results showing a minimal role for the eIF4F complex in viral mRNA translation, we found that depleting eIF4G prior to infection did not impact IE1 and IE2 translation. Together, our results define a new role for DHX29 in regulating eIF4F-dependent translation and identify a critical role for DHX29 in the translation of HCMV mRNAs. - Source: PubMed
Publication date: 2026/06/09
Lenarcic Erik MMoorman Nathaniel J - The roles of translational control in the immune system are incompletely understood. Using a CRISPR/Cas9-mediated functional screen of RNA helicases in an in vitro system of plasma cell differentiation, we identify in this study DHX29 as a critical regulator of this process. Mice with B-cell-specific deletion of Dhx29 exhibit severely impaired germinal center B-cell formation, plasma cell differentiation, and antibody production. Mechanistically, DHX29 promotes translation of Tcf3 and Tle3 mRNAs via binding to their 5' untranslated regions (UTRs). In the absence of DHX29, B cells exhibit normal proliferation but fail to undergo class switch to IgG1 and differentiation into plasma cells, resulting in impaired antibody production. Ectopic expression of TCF3 and TLE3 largely restores plasma cell differentiation of Dhx29-deficient B cells. Our study provides insights into the functional importance of translational control in the immune system by unraveling critical roles of the RNA helicase DHX29 in the translation of key transcription factors controlling germinal center response and plasma cell differentiation. - Source: PubMed
Publication date: 2026/05/26
Zhao JiayiHe XiaoyuHong PeichengLin LianghuaDu YingChen PengdaZhang LixiaoLeng JialeMa LihuiXie JunLin XinyongAdilijiang AbidanWang JiazhenHong YazhenXiao ZhengtaoLiu Wen-HsienXiao Changchun - Pre-mRNA splicing produces intron lariats that must be cleaved at their internal 2-5' phosphodiester bond by the debranching endonuclease DBR1. While human DBR1 (hDBR1) is established as the lariat debranching enzyme, how it interfaces with broader RNA metabolic pathways is less clear. Using chemical inhibition of splicing, we show that DBR1 expression correlates with splicing activity. We then mapped the hDBR1 interactome by immunopurification coupled to mass spectrometry using complementary gel-based and on-bead workflows. hDBR1 associates with the spliceosome and intron-turnover factors, and with RNA quality-control proteins, including UPF1, XRN2, and the RNA helicase DHX29. RNase A treatment identifies an RNA-dependent subnetwork enriched for stress-granule proteins and hnRNPs, linking hDBR1 to RNA surveillance during stress. Comparison with BioGRID indicates that most detected associations were not previously reported. Finally, phosphoproteomic profiling reveals multiple hDBR1 phosphorylation sites, including four residues preferentially detected after RNase treatment, suggesting regulatory modifications that may tune hDBR1 interactions or activity. Together, these data expand the functional landscape of hDBR1 across splicing, intron turnover, and RNA quality control. - Source: PubMed
Publication date: 2026/04/16
Barwell TiffanyGautam DipendraNitika Zheng BoTruman Andrew WChakrabarti Kausik - Synonymous codon usage controls global gene expression in both prokaryotic and eukaryotic species. Nonoptimal codons are known to induce messenger RNA (mRNA) decay; however, the underlying molecular mechanism remains poorly understood in human cells. Through genome-wide CRISPR screening, we identified the RNA binding protein DHX29 as a critical regulator of codon-dependent gene expression. Cryo-electron microscopy and selective ribosome profiling demonstrated that DHX29 directly interacts with the A-site entrance of the translating 80 ribosome, the binding site for the eEF1A•GTP•aminoacyl-tRNA ternary complex, suggesting a role in monitoring aminoacyl-tRNA sampling. Proteomic analysis further revealed that DHX29 recruits the GIGYF2•4EHP complex to mediate global suppression of nonoptimal mRNAs. These findings establish a mechanistic link between synonymous codon usage and the regulation of gene expression. - Source: PubMed
Publication date: 2026/05/07
Hia FabianWu YitongYoshinaga MasanoriGoto-Ito SakurakoIwasaki WakanaImami KoshiToh HirotakaHan PeixunCai TingOhira TakayukiFukao AkiraStandley Daron MShichino YuichiTakegawa MasakiFujiwara ToshinobuSuzuki TsutomuIwasaki ShintaroBassik Michael CIto TakuhiroTakeuchi Osamu