These findings indicate that the OP-1 device has the potential for initiating bone formation in the human maxillary sinus within 6 months after a sinus floor elevation operation. However, the various findings in these 3 patients indicate that the behaviour of the material is at this moment insufficiently predictable, in this indication area. Further investigation is indicated before OP-1 can be successfully used instead of the "gold standard" autogenous bone graft.
Mutually exclusive splicing of exons 6A and 6B from the chicken -tropomyosin gene involves numerous regulatory sequences. Previously, we identified a G-rich intronic sequence (S3) downstream of exon 6B. This element consists of six G-rich motifs, mutations of which abolish splicing of exon 6B. In this paper, we investigated the cellular factors that bind to this G-rich element. By using RNA affinity chromatography, we identified heterogeneous nuclear ribonucleoprotein (hnRNP) A1, the SR proteins ASF/SF2 and SC35, and hnRNP F/H as specific components that are assembled onto the G-rich element. By using hnRNP A1-depleted HeLa nuclear extract and add-back experiments, we show that hnRNP A1 has a negative effect on splicing of exon 6B. In agreement with in vitro data, artificial recruitment of hnRNP A1, as a fusion with the MS2 coat protein, also represses splicing of exon 6B ex vivo. In contrast, ASF/SF2 and SC35 activate splicing of exon 6B. As observed with other systems, hnRNP A1 counteracts the stimulating effect of the SR proteins. Moreover, cross-linking experiments show that both ASF/SF2 and SC35 are able to displace binding of hnRNP A1 to the G-rich element, suggesting that the binding sites for these proteins are overlapping. These data indicate that the G-rich sequence is a composite element that acts as an enhancer or as a silencer, depending on which proteins bind to them. Splicing is the process by which introns from premessenger RNAs are removed in eukaryotes. Pre-mRNA splicing takes place within the spliceosome, which is a large, highly dynamic complex composed of four small ribonucleoprotein particles (snRNP 1 U1, U2, U4/U6, and U5) and multiple non-snRNP factors (1, 2). One of the most intriguing questions that remains in RNA splicing is how the 5Ј and 3Ј splice sites are selected and paired together within large RNA sequences (3). This question takes on particular importance in alternative splicing, where the selection of certain splice sites is modulated depending on the developmental stage, on tissue differentiation, or on metabolic changes of the cells (3). Numerous studies have demonstrated that regulatory sequences within the pre-mRNA that lie outside the splicing signals play a crucial role in controlling the choice of splicing sites in a given cellular context (reviewed in Refs. 4 and 5).Among these sequences are the splicing enhancers. These elements are found in a wide variety of metazoan pre-mRNAs, either within exons or introns. Purine-rich splicing enhancers (known as ESE) are a well characterized class of exonic splicing enhancers that mostly interact with specific subsets of SR proteins (reviewed in Refs. 6 and 7). SR proteins belong to a family of essential splicing factors that are highly conserved between Drosophila and mammals and that are involved in both constitutive and regulated splicing events (reviewed in Refs. 8 and 9). It has been proposed that the function of SR proteins is to stimulate the recognition of weak upstream 3Ј splice sites, by recruiting U2AF 65/35 , or to f...
We have determined the nucleotide sequence of group II RNA phage KU1. The most conspicuous difference in the comparison with other group II members such as GA and JP34 is the presence of an insertion in the start codon of the lysis gene. In GA and JP34, the coat and lysis genes overlap by one nucleotide in the configuration UAAUG. The 18-nt insertion in KU1 is positioned between the A and the U of the start codon. It does not affect the coat reading frame, but it destroys the AUG start codon and separates the previously overlapping genes by 17 nts. The insert creates a UUG codon at its 3' border which serves as the start site for lysis protein synthesis in KU1. We also show that analogous to the group I phages, such as MS2 and fr, expression of the lysis gene in KU1 and JP34 is coupled to termination of translation at the coat gene. RNA secondary structure models for the central parts of KU1 and JP34 are suggested which can account for the insertion as a separate stem-loop structure.
Hybrids between different species or genera of the single-stranded RNA coliphages have not been found in nature. Here, it has been shown that viable hybrids between different phage species can easily be generated in the laboratory by in vivo recombination. cDNA of species I phage MS2 located on a plasmid and lacking part of its 5h untranslated leader (5h UTR) was complemented with another plasmid carrying the 5h half of the genome of fr, a species I phage, or of KU1, a species II representative with low sequence similarity. When the two plasmids were present in the same cell there was spontaneous production of hybrid phages. Interestingly, these hybrids did not arise by a double or single crossover that would replace the missing MS2 sequences with those of fr or KU1. Rather, hybrids arose by attaching the complete 5h UTR of fr or KU1 to the 5h terminus of the defective MS2 phage. Several elements of the 5h UTR then occurred twice, one from KU1 (or fr) and the other from MS2. These redundant elements are in most cases deleted upon evolution of the hybrids. As a result, the 5h UTR of KU1 (or fr) then replaced that of MS2. It was earlier shown that this 5h UTR could assume two alternating structures that facilitated transient translation of the proximal maturation gene. Apparently, this timer function of the 5h UTR was exchangeable and could function independently of the rest of the genome. When hybrids were competed against wildtype, they were quickly outgrown, probably explaining their absence from natural isolates.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.