Genomes and Genes
Gene Symbol: TXNL4A
Description: thioredoxin like 4A
Alias: BMKS, DIB1, DIM1, SNRNP15, TXNL4, U5-15kD, thioredoxin-like protein 4A, DIM1 protein homolog, spliceosomal U5 snRNP-specific 15 kDa protein, thioredoxin-like 4, thioredoxin-like U5 snRNP protein U5-15kD
- Pessa H, Will C, Meng X, Schneider C, Watkins N, Perälä N, et al. Minor spliceosome components are predominantly localized in the nucleus. Proc Natl Acad Sci U S A. 2008;105:8655-60 pubmed publisher..Thus, our data, combined with several earlier publications, establish that, like the major spliceosome, components of the U12-dependent spliceosome are localized predominantly in the nucleus. ..
- Johnson M, Ghalei H, Doxtader K, Karbstein K, Stroupe M. Structural Heterogeneity in Pre-40S Ribosomes. Structure. 2017;25:329-340 pubmed publisher..These models are supported by biochemical analyses using point variants and suggest that maturation of the 18S 3' end is regulated by dissociation of the AF Dim1 from the subunit interface, consistent with previous biochemical analyses.
- Mizuguchi M, Obita T, Kajiyama A, Kozakai Y, Nakai T, Nabeshima Y, et al. Allosteric modulation of the binding affinity between PQBP1 and the spliceosomal protein U5-15kD. FEBS Lett. 2016;590:2221-31 pubmed publisher..Our results suggest that the interaction between PQBP1 and WBP11 negatively modulates the U5-15kD binding of PQBP1 by an allosteric mechanism. ..
- Goos J, Swagemakers S, Twigg S, van Dooren M, Hoogeboom A, Beetz C, et al. Identification of causative variants in TXNL4A in Burn-McKeown syndrome and isolated choanal atresia. Eur J Hum Genet. 2017;25:1126-1133 pubmed publisher..Recently, causative compound heterozygous variants were identified in TXNL4A. We analyzed an individual with clinical features of BMKS and her parents by whole-genome sequencing and ..
- Hussain A, Tian M, Wen S. Exploring the Caste-Specific Multi-Layer Defense Mechanism of Formosan Subterranean Termites, Coptotermes formosanus Shiraki. Int J Mol Sci. 2017;18: pubmed publisher..i>CAT, GST, PRXSL, Cu/Zn-SOD2, TXN1, TXN2, TXNL1, TXNL2, TXNL4A and TPx genes among winged imagoes upon infection with the most virulent isolate, M...
- Jin T, Guo F, Wang Y, Zhang Y. Identification of human dim1 as a peptidase with autocleavage activity. Chem Biol Drug Des. 2006;68:266-72 pubmedb>Dim1 is a highly conserved splicing factor. It is encoded by an essential gene in fission yeast and the Caenorhabditis elegans. It may also be involved in tissue-specific or pathway-specific alternative splicing...
- Zhang Y, Cheng H, Gould K, Golemis E, Roder H. Structure, stability, and function of hDim1 investigated by NMR, circular dichroism, and mutational analysis. Biochemistry. 2003;42:9609-18 pubmed..Other residues essential for hDim1 function are identified by using mutational and genetic approaches. The residues thus identified are not identical with those previously shown to govern Dim1 interaction with defined protein partners.
- Wieczorek D, Newman W, Wieland T, Berulava T, Kaffe M, Falkenstein D, et al. Compound heterozygosity of low-frequency promoter deletions and rare loss-of-function mutations in TXNL4A causes Burn-McKeown syndrome. Am J Hum Genet. 2014;95:698-707 pubmed publisher..We identified biallelic mutations in TXNL4A, a member of this complex, in individuals with Burn-McKeown syndrome (BMKS)...
- Liu S, Rauhut R, Vornlocher H, Luhrmann R. The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP. RNA. 2006;12:1418-30 pubmed..Taken together, data presented here provide a detailed picture of the network of protein interactions within the human tri-snRNP. ..
- Zhang Y, Gould K, Dunbrack RL J, Cheng H, Roder H, Golemis E. The evolutionarily conserved Dim1 protein defines a novel branch of the thioredoxin fold superfamily. Physiol Genomics. 1999;1:109-18 pubmedb>Dim1 is a small evolutionarily conserved protein essential for G2/M transition that has recently been implicated as a component of the mRNA splicing machinery...
- Bertram K, Agafonov D, Dybkov O, Haselbach D, Leelaram M, Will C, et al. Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for Activation. Cell. 2017;170:701-713.e11 pubmed publisher..These include formation of a partially closed Prp8 conformation that creates, together with Dim1, a 5' splice site (ss) binding pocket, displacement of Sad1, and rearrangement of Brr2 such that it contacts its U4/..
- Gilmore Hebert M, Ramabhadran R, Stern D. Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage response pathways. Mol Cancer Res. 2010;8:1388-98 pubmed publisher..Overall, these findings further substantiate the role of ErbB4 in conjoint regulation of growth factor signaling and DNA damage responses. ..
- Takahashi M, Mizuguchi M, Shinoda H, Aizawa T, Demura M, Okazawa H, et al. Polyglutamine tract-binding protein-1 binds to U5-15kD via a continuous 23-residue segment of the C-terminal domain. Biochim Biophys Acta. 2010;1804:1500-7 pubmed publisher..These findings suggest that the frameshift mutations in the PQBP-1 gene lead to expression of mutants lacking the ability to interact with U5-15kD. ..
- Ghalei H, Trepreau J, Collins J, Bhaskaran H, Strunk B, Karbstein K. The ATPase Fap7 Tests the Ability to Carry Out Translocation-like Conformational Changes and Releases Dim1 during 40S Ribosome Maturation. Mol Cell. 2017;67:990-1000.e3 pubmed publisher..of the rotated state, a key intermediate in translocation, thereby releasing the essential assembly factor Dim1 from pre-40S subunits. Bypassing this quality control step produces defects in reading frame maintenance...
- Laggerbauer B, Liu S, Makarov E, Vornlocher H, Makarova O, Ingelfinger D, et al. The human U5 snRNP 52K protein (CD2BP2) interacts with U5-102K (hPrp6), a U4/U6.U5 tri-snRNP bridging protein, but dissociates upon tri-snRNP formation. RNA. 2005;11:598-608 pubmed..The interaction of 52K with a tri-snRNP bridging protein, coupled with its absence from the tri-snRNP, suggests it might function in tri-snRNP assembly. ..
- Zhang Y, Lindblom T, Chang A, Sudol M, Sluder A, Golemis E. Evidence that dim1 associates with proteins involved in pre-mRNA splicing, and delineation of residues essential for dim1 interactions with hnRNP F and Npw38/PQBP-1. Gene. 2000;257:33-43 pubmed..U5 tri-snRNP, required for pre-mRNA splicing. To investigate the mechanism(s) of Dim1 function, reiterative two-hybrid screening was performed to identify interacting proteins...
- Waragai M, Junn E, Kajikawa M, Takeuchi S, Kanazawa I, Shibata M, et al. PQBP-1/Npw38, a nuclear protein binding to the polyglutamine tract, interacts with U5-15kD/dim1p via the carboxyl-terminal domain. Biochem Biophys Res Commun. 2000;273:592-5 pubmed..This finding suggests physiological functions of PQBP-1 in splicing, cell cycle, and ubiquitination, through which we can speculate the pathological roles of PQBP-1 in triplet repeat diseases. ..