Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.30.1 (S1 nuclease)
 3,660 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Inhibin and activin are best known as gonadal glycoprotein hormones but have a broad anatomical distribution. We previously described the central distribution ofinhibin/activin beta A- and beta B-subunit proteins in some neuronal cell bodies, fibers, and nuclei of the rat brain and reported a possible role for central activin in suckling-induced oxytocin secretion and corticotropin releasing factor release. In the present report, we mapped the detailed immunohistochemical localization of inhibin/activin alpha-, beta A-, and beta B-subunits throughout the rat brain to further clarify their central distribution. In addition, the localization and distribution of their corresponding mRNAs was assessed. The results are summarized as follows: 1) Both beta A- and beta B-subunit immunoreactivity are found in neuronal cell bodies in the nucleus of the solitary tract and the dorsal and ventral medullary reticular nuclei, and in fibers and terminals of known projection sites for these nuclei. 2) beta B-subunit immunoreactivity is localized in a group of perifornical neurons in the hypothalamus. 3) beta A-subunit immunoreactivity is present in discrete populations of neuronal cell nuclei scattered throughout the CNS. 4) mRNAs encoding each of the inhibin/activin subunits are expressed in all major brain regions as determined by S1 nuclease assay and in a variety of specific neuroanatomical sites as shown by in situ hybridization. The results suggest that central inhibin and activin proteins are produced in the brain where they may potentially serve inter- and intracellular functions in multiple systems.
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PMID:Hybridization histochemical and immunohistochemical localization of inhibin/activin subunits and messenger ribonucleic acids in the rat brain. 882 Aug 78

We have previously reported that the expression of HC gp-39, a 39-kDa secretory glycoprotein and member of the chitinase protein family, is associated with late stages of monocyte to macrophage maturation. To allow further investigations of its unique expression pattern and to facilitate studies on the regulation of this "marker gene," we characterized the genomic organization of the HC gp-39 gene (HGMW-approved symbol CHI3L1) and cloned its 5'-proximal promotor region. The gene is composed of 10 exons distributed over an 8-kb region. Two transcriptional initiation sites located 82 and 126 nucleotides upstream of the ATG start codon were identified using primer extension and S1 nuclease protection assays. We sequenced 1.3 kb of the 5'-flanking region and identified a variety of putative regulatory elements.
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PMID:Molecular characterization of the gene for human cartilage gp-39 (CHI3L1), a member of the chitinase protein family and marker for late stages of macrophage differentiation. 924 40

The genomic structure of the human CD94 gene was obtained by analyzing genomic clones obtained from two different libraries. The CD94 gene contains six exons separated by five introns. The carbohydrate-recognition domain (CRD) is encoded by three exons, and the conservation of intron positions within the CRD indicated that CD94 is closely related to group V of C-type lectins. Primer extension and S1 nuclease protection assays showed that initiation of transcription in the CD94 gene is heterogeneous, but restricted to a 60 base pair region around the major initiation site enclosed within a putative initiator element (TTA+1TTCA). The study of the promoter region of CD94 may help to understand the selective expression of this C-type lectin glycoprotein on NK cells and subsets of cytotoxic T cells.
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PMID:Structure of the human CD94 C-type lectin gene. 947 66

We established the transcription map of early region (E) 3 of bovine adenovirus 3 (BAV-3) by Northern blot, S1 nuclease protection assays, cDNA sequencing, and RT-PCR analysis. Five major classes of mRNAs were identified, which shared the 3' ends. Four classes of mRNAs transcribed from the E3 promoter also shared the 5' end, while one major class of mRNA transcribed from the major late promoter contained a tripartite leader sequence at the 5' end. These five transcripts have the potential to encode four proteins, namely 284R, 121R, 86R, and 82R. To identify the proteins, rabbit antiserum was prepared using a bacterial fusion protein encoding 284R or 121R protein. Serum against 284R immunoprecipitated protein of 26-32 kDa in in vitro translated and transcribed mRNA and three proteins of 48, 67, and 125 kDa from BAV-3-infected cells. Western blots and enzymatic digestions confirmed that the 284R protein is a glycoprotein, which contains only N-linked oligosaccharides, both high mannose (48 kDa) and complex types (67 kDa). Serum against 121R immunoprecipitated a protein of 14.5 kDa from in vitro translated and transcribed mRNA and BAV-3-infected cells. Although 121R protein shows limited sequence similarity to a 14.7-kDa protein of human adenovirus 5, the 284R protein appears to be unique to BAV-3. Since proteins encoded by the E3 region appear to influence adenovirus pathogenesis, the 284R protein may contribute to the unique pathogenic properties of BAV-3.
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PMID:Transcription mapping and characterization of 284R and 121R proteins produced from early region 3 of bovine adenovirus type 3. 1019 Dec

Early region 4 (E4) of bovine adenovirus type 3 (BAV-3) was analyzed by Northern blotting, RT-PCR analysis, cDNA sequencing, and S1 nuclease protection assays. The transcriptional map of the E4 region of BAV-3 has marked dissimilarities from those of mouse adenovirus-1, ovine adenovirus-287, and human adenovirus-2, for which the transcriptional maps have been constructed. The E4 region of BAV-3, located between 98.6 and 89.8 MU transcribes seven distinct classes of bovine adenovirus type 3 mRNA. The seven mRNA species formed by the removal of one to three introns share both the 3' end and a short 5' leader (25 nucleotides). The E4 mRNAs can encode at least five unique polypeptides, namely, 143R1, 69R, 143R2, 268R, and 219R. Isolation of a replication-competent recombinant "BAV404" containing 1.9-kb insertion [glycoprotein (gD) of bovine herpesvirus 1, under the control of a SV40 early promoter and poly(A)] in the region between E4 and the right ITR suggested that this region is nonessential for BAV-3 replication. Expression of gD by BAV404 recombinant virus was confirmed by immunoprecipitation with gD-specific monoclonal antibodies. Analysis of the kinetics of protein expression indicated that gD is expressed at both early and late times postinfection. These results suggest that: (a) E4 produces seven 5'-3' coterminal mRNAs and (b) the right terminal region of BAV-3 can be used for the expression of vaccine antigens.
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PMID:Transcription map and expression of bovine herpesvirus-1 glycoprotein D in early region 4 of bovine adenovirus-3. 1044 62

We investigated the cis-acting sequences of the promoter regulating the gene encoding the glycoprotein C (gC) of bovine herpesvirus 1 (BoHV-1), a gene of the gamma1 class. S1 nuclease protection assays revealed that gC transcription initiated predominantly at position C18281 of the viral genome, corresponding to 21 and 56 bases downstream from putative TATA-like and CAAT boxes, respectively. To map the gC promoter (pgC), we measured the ability of a series of nested deletions of the region +71 to -1155 with respect to the major gC transcriptional start site, to drive expression of the firefly luciferase (Luc) reporter gene following transient transfection of a cell host, in the absence as well as in the presence of viral factors expressed in trans. We show that the minimal pgC sequences required to drive maximal BoHV-1 independent expression was within the region +71 to -76 which harbours the putative TATA and CAAT boxes, the mRNA start site, and the complete 5' transcript leader sequence. This small pgC fragment was highly trans-activated by the co-expression of the BoHV-1-encoded BICP27 protein, but not BICP0 nor BTIF. In contrast, the pgC fragment spanning the region +71 to -1155 was only minimally trans-activated by BICP27, but substantially stimulated by BICP0. These findings thus suggest that gC gene regulation may involve the combined action of several viral transactivators.
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PMID:Mapping of the bovine herpesvirus 1 glycoprotein C promoter region and its specific transactivation by the viral BICP27 gene product. 1253

The multi S1/P1 nuclease AtBFN2 (EC 3.1.30.1) encoded by the Arabidopsis thaliana At1g68290 gene is a glycoprotein that digests RNA, ssDNA, and dsDNA. AtBFN2 depends on three zinc ions for cleaving DNA and RNA at 3'-OH to yield 5'-nucleotides. In addition, AtBFN2's enzymatic activity is strongly glycan dependent. Plant Zn(2+)-dependent endonucleases present a unique fold, and belong to the Phospholipase C (PLC)/P1 nuclease superfamily. In this work, we present the first complete, ligand-free, AtBFN2 crystal structure, along with sulfate, phosphate and ssDNA co-crystal structures. With these, we were able to provide better insight into the glycan structure and possible enzymatic mechanism. In comparison with other nucleases, the AtBFN2/ligand-free and AtBFN2/PO4 models suggest a similar, previously proposed, catalytic mechanism. Our data also confirm that the phosphate and vanadate can inhibit the enzyme activity by occupying the active site. More importantly, the AtBFN2/A5T structure reveals a novel and conserved secondary binding site, which seems to be important for plant Zn(2+)-dependent endonucleases. Based on these findings, we propose a rational ssDNA binding model, in which the ssDNA wraps itself around the protein and the attached surface glycan, in turn, reinforces the binding complex.
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PMID:Structural insights of the ssDNA binding site in the multifunctional endonuclease AtBFN2 from Arabidopsis thaliana. 2515 44


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