Disease relevance of UTS2D

• Experiments with a mixture of recombinant phage displaying U1A or the closely related protein U2B" demonstrated that addition of a competitor RNA can suppress selection of a protein with a higher affinity for a given RNA target, thereby allowing the preferential amplification of a lower affinity protein [1].
• The peak ANP level occurred significantly later in the URP group (69 +/- 16 hours) than in the SRP group (28 +/- 9 hours, P < .001) after the onset of infarction [2].
• In conclusion, MTS and U2B methods are equally useful in the diagnosis of microsporidiosis [3].

High impact information on UTS2D

• In contrast to import mediated by members of the importin-beta family of nucleocytoplasmic transport receptors, U1A/U2B" import is not inhibited by either nonhydrolyzable guanosine triphosphate (GTP) analogues or by a mutant of the GTPase Ran that is incapable of GTP hydrolysis [4].
• Adenosine triphosphate is capable of supporting U1A and U2B" import, whereas neither nonhydrolyzable adenosine triphosphate analogues nor GTP can do so [4].
• An ATP-dependent, Ran-independent mechanism for nuclear import of the U1A and U2B" spliceosome proteins [4].
• These patients had proximal occlusion of the dominant right coronary artery involving the right atrial branches: 9 patients with successful reperfusion (SRP group) and the remaining 11 patients with unsuccessful reperfusion (URP group) [2].
• It binds in vitro to its RNA target, U2 snRNA stem-loop IV, without a protein cofactor, and the target resembles more closely the U1 snRNA binding site of the human U1A protein than it does the U2 snRNA binding site of human U2B". Surprisingly, the YU2B" protein lacks a C-terminal RNA binding domain, which is conserved in all other family members [5].

Biological context of UTS2D

• Structure-activity relationships and structural conformation of a novel urotensin II-related peptide [6].
• Here we investigate nuclear import of U1A and U2B" in vitro and demonstrate that it occurs by an active, saturable process [4].
• We have compared the effect on RNA binding of multiple double point mutations at analogous positions in the U1A and U2B" protein [7].
• The regions homologous to the U2-B" gene are not limited to single exons and are mostly not confined by exon-exon junctions in the corresponding U1-A mRNA [8].
• The amino acid sequences of the two peptides, designated UIIA and UIIB, are as follows: UIIA, H-Gly-Ser-Gly-Ala-Asp-Cys-Phe-Trp-Lys-Tyr-Cys-Val-OH; UIIB, H-Gly-Ser-Asn-Thr-Glu-Cys-Phe-Trp-Lys-Tyr-Cys-Val-OH [9].

Anatomical context of UTS2D

• The prepro-URP gene is expressed in several rat tissues, although with lower levels than the prepro-UII gene and, in the human, is expressed comparably to prepro-UII in several tissues except the spinal cord [10].

Associations of UTS2D with chemical compounds

• Alanine substitution of each residue of URP significantly reduced the binding affinity and the contractile activity of the peptides, except for the Ala8-substituted analog that retained biological activity [6].
• Target discrimination by RNA-binding proteins: role of the ancillary protein U2A' and a critical leucine residue in differentiating the RNA-binding specificity of spliceosomal proteins U1A and U2B" [11].
• However, the proline-rich region of U1-A, absent in U2-B", is encoded by a single exon, suggesting a specific function for this domain of U1-A [8].

Regulatory relationships of UTS2D

• Most importantly, D-scan of URP revealed that [D-Trp4]URP abrogated and [D-Tyr6]URP partially suppressed the UII-evoked contractile response [6].

Other interactions of UTS2D

• These results suggest that URP is the endogenous and functional ligand for UII receptor in the rat and mouse, and possibly in the human [12].

Analytical, diagnostic and therapeutic context of UTS2D

• Furthermore, using surface plasmon resonance (SPR) technology, we measured the binding affinities of the ligands, U-II, URP, and urantide toward the UT extracellular segments [13].
• In order to study the structure-function relationships of URP, we have synthesized a series of URP analogs and measured their binding affinity on hGPR14-transfected cells and their contractile activity in a rat aortic ring bioassay [6].
• To analyze the organization of spliceosomal snRNPs in plant nuclei, we have used both immunofluorescence labelling with the antibody 4G3, raised against the human snRNP-specific protein U2B", and in situ hybridization with anti-sense probes to conserved regions of U1, U2 and U6 snRNAs [14].

References