Ask about this productRelated genes to: RNASE11 antibody
- Gene:
- RNASE11 NIH gene
- Name:
- ribonuclease A family member 11 (inactive)
- Previous symbol:
- C14orf6
- Synonyms:
- RAJ1
- Chromosome:
- 14q11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2002-11-27
- Date modifiied:
- 2018-02-07
Related products to: RNASE11 antibody
Related articles to: RNASE11 antibody
- Sperm small RNAs are implicated in intergenerational transmission of paternal environmental effects. Small RNAs generated by the cleavage of tRNAs, known as tRNA fragments (tRFs) or tRNA-derived RNAs (tDRs or tsRNAs), are an abundant class of RNAs in mature sperm and can be modulated by environmental conditions. The biogenesis of tRFs in the male reproductive tract remains poorly understood. Angiogenin, a member of the ribonuclease A superfamily (RNase A), cleaves tRNAs to generate tRFs in response to cellular stress. Four paralogs of Angiogenin, namely Rnase9, Rnase10, Rnase11, and Rnase12, are specifically expressed in the epididymis-a long, convoluted tubule where sperm mature and acquire fertility and motility. Here, by generating mice deleted for all four genes (Rnase9-12-/-, termed "KO" for Knock Out), we report that these genes regulate fertility and small RNA levels. KO male mice are sterile; KO sperm fertilized oocytes in vitro but failed to efficiently fertilize oocytes in vivo due to an inability of sperm to pass through the utero-tubular junction. Intriguingly, there were decreased levels of tRFs and rRNAs (rRNA-derived small RNAs or rsRNAs) in the KO epididymis and epididymal luminal fluid, although RNases 9-12 did not show ribonucleolytic activity in vitro. Importantly, KO sperm showed a dramatic decrease in the levels of tRFs, demonstrating a role of epididymis-specific Rnase9-12 genes in regulating sperm small RNA composition. Together, our results reveal an unexpected role of four epididymis-specific noncanonical ribonuclease A family genes in regulating fertility and small RNA processing. - Source: PubMed
Publication date: 2024/10/28
Shaffer Joshua FGupta AlkaKharkwal GeetikaLinares Edgardo EHolmes Andrew DSwartz Julian RKatzman SolSharma Upasna - Sperm small RNAs are implicated in intergenerational transmission of paternal environmental effects. Small RNAs generated by cleavage of tRNAs, known as tRNA fragments (tRFs), are an abundant class of RNAs in mature sperm, and can be modulated by environmental conditions. The ribonuclease(s) responsible for the biogenesis of tRFs in the male reproductive tract remains unknown. Angiogenin, a member of the Ribonuclease A superfamily (RNase A), cleaves tRNAs to generate tRFs in response to cellular stress. Four paralogs of Angiogenin, namely , , and , are specifically expressed in the epididymis-a long, convoluted tubule where sperm mature and acquire fertility and motility. The biological functions of these genes remain largely unknown. Here, by generating mice deleted for all four genes (/, termed "KO" for Knock Out), we report that these genes regulate fertility and RNA processing. KO mice showed complete male sterility. KO sperm fertilized oocytes but failed to efficiently fertilize oocytes , likely due to an inability of sperm to pass through the utero-tubular junction. Intriguingly, there were decreased levels of fragments of tRNAs (tRFs) and rRNAs (rRNA-derived small RNAs or rsRNAs) in the KO epididymis and epididymal luminal fluid, implying that regulate the biogenesis and/or stability of tRFs and rsRNAs. Importantly, KO sperm showed a dramatic decrease in the levels of tRFs, demonstrating a role of in regulating sperm RNA composition. Together, our results reveal an unexpected role of four epididymis-specific non-canonical RNase A family genes in fertility and RNA processing. - Source: PubMed
Publication date: 2024/08/27
Shaffer Joshua FGupta AlkaKharkwal GeetikaLinares Edgardo EHolmes Andrew DKatzman SolSharma Upasna - The structural motif of 'product conformation driven V8 protease catalyzed ligation reaction' can be represented by FR(I)-EALER-FR(II). The relative roles of the flanking regions (FR(I) and FR(II)) and of splicedon, the central penta-peptide, on the thermodynamic stability of the 'conformational trap' of the product has been now evaluated as a function of co-solvent concentration. The studies have established that the thermodynamic stability of the conformational trap of alpha17-40des23-26 with four different splicedons (EALER, EALEV, EYGER, or EGAER) that differ in the intrinsic alpha-helical potential of their amino acid residues and/or ability to generate i, i+4 side chain interaction is a direct correlate of the n-propanol induced alpha-helical conformation of the product. On the other hand, when the product is defined by only splicedon EALER, and the flanking regions are disitinct; no correlation could be drawn between the stability of the trap and solvent induced alpha-helical conformation, even though these generally give an equilibrium yield of 45% in 30% n-propanol and is not influenced by an increased propanol concentration. However, when the splicedon EALER with given FR(I) and FR(II) region develops a 'conformational trap' of a lower stability in 30% propanol as seen with beta18-25(A22)-EALER-beta31-39, the stability increases in 60% n-propanol, without significant increase in the alpha- helical conformation. Though, primary structure of RNAse1-20, could be presented as RNAse1-5-AKFER- RNAse1-20, and alpha-helical conformation is induced to this peptide both in 30 and 60% propanol, splicedon AKFER by itself does not develop the 'conformational trap' of RNAse1-20. The splicedon AKFER of RNAse1-20 fails to develop the 'conformational trap', due to an intrinsic inhibitory potential of its FR region, RNAse11-20; replacing RNAse11-20 with alpha32-40 enables the splicedon AFKER to generate the 'conformational trap'. The studies presented here have demonstrated the primary role of flanking regions in establishing the amount of the solvent induced alpha-helical conformation and that of the splicedon in dictating the thermodynamic stability of its 'conformational trap' of the products, nonetheless one influences the other to some degree. We suggest that the stability of the 'conformational trap' of the product reflects the ability of the splicedon to 'recruit' the product conformation to protect the spliced peptide bond, i.e. to reduce the helix-coil transition of the spliced region which in turn imparts a degree of resistance to the spliced peptide bond. - Source: PubMed
Srinivasulu SonatiAcharya A Seetharama