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

Analysis of the temporal sequence of RNA transcription within the Autographa californica nuclear polyhedrosis virus genome revealed individual transcription units composed of overlapping early or late RNAs, or both. High-resolution S1 nuclease mapping within the 3.0-kilobase HindIII-K fragment located five overlapping RNAs (1.07, 1.38, 2.63, 3.16, and 3.50 kilobases) transcribed in the same direction and terminated at a common 3' site. The smallest RNAs appeared early but were replaced in time by successively larger RNAs initiated further upstream. Primer extension analysis supported the contention that this temporal regulation involved the sequential activation of upstream promoters and the coordinate deactivation of downstream promoters. As such, transcription from upstream genes may suppress that of downstream genes via transcriptional interference (promoter occlusion) and thereby facilitate sequential expression of different viral functions. In contrast, overlapping RNAs with extended 3' ends were transcribed from the abundantly expressed p10 and polyhedrin genes mapping to the HindIII-Q,P/EcoRI-P and HindIII-V/EcoRI-I fragments, respectively. These RNAs were synthesized maximally during the very late occlusion phase and consisted of a major small transcript and several larger but less abundant transcripts.
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PMID:Temporal regulation of baculovirus RNA: overlapping early and late transcripts. 388 31

Intracytoplasmic A particles (CAP), previously identified as probably cytoplasmic nucleocapsid precursor structures to mouse mammary tumour virus (MMTV), possess both DNA binding and DNA unwinding activities, CAP proteins bind to both single-stranded (ss)- and double-stranded (ds)DNA, with the ssDNA slightly preferred. This activity was linear over a 30-fold concentration of A particle protein and was not affected by NaCl concentrations as high as 0.6 M or pH changes over a wide range. DNA binding by CAP proteins was sensitive to heat or addition of sodium dodecyl sulphate (SDS) and was neutralized by pre-incubation of CAP with anti-MMTV p14, but not by anti-MMTV p27, p10 or anti-mouse casein. Incubation of CAP with dsDNA led to unwinding of the double helix as measured by its increased sensitivity to S1 nuclease digestion. This activity was also linear over a several-fold concentration of A particle protein and was heat labile. It was not inhibited by pre-incubation of CAP with either anti-MMTV p14 or with anti-MMTV, anti-MMTV p27 and anti-MMTV p10. DNA unwinding was inhibited by anti-A particle antiserum and to a lesser extent by anti-CAP p20-18.
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PMID:DNA binding and unwinding activities associated with intracytoplasmic a particles isolated from mouse mammary tumors. 625 67

The structures of murine sarcoma virus (MuSV) ts110 viral RNA and intracellular RNA present in MuSV ts110-infected cells (6m2 cells) have been examined by S1 nuclease analysis. A previous study involving heteroduplex analysis of MuSV ts110 viral RNAs hybridized to wild-type DNA revealed the presence of two MuSV ts110 RNAs, 4.0 and 3.5 kilobases (kb) in length, containing overlapping central deletions relative to wild-type MuSV 124 viral RNA (Junghans et al., J. Mol. Biol. 161:229-255, 1982). Here we show that the deletion (termed delta 1) in the 4.0-kb RNA has a 5' border located at about nucleotide 2409 (using the numbering system of Van Beveren et al., Cell 27:97-108, 1981), a position 63 bases upstream of the junction of the p30 and p10 coding sequences. The 3' border of the delta 1 deletion is found 1,473 bases downstream at approximately nucleotide 3883, 10 nucleotides downstream of the first mos gene initiation codon. In the 3.5-kb MuSV ts110 RNA, the 5' border of the deleted central region (termed delta 2) is located in a splice consensus donor site at approximately nucleotide 2017, 330 bases downstream from the junction of the p12 and p30 coding sequences, and extends about 1,915 bases in the downstream direction to nucleotide 3935, found in a splice consensus acceptor site about 55 nucleotides downstream of the first mos gene initiation codon and 30 bases upstream of the second initiation codon. No alteration of polyadenylate addition sites was observed in either MuSV ts110 RNA species, as compared with MuSV 349 RNA. The observation that the 5' and 3' borders of the deletion in the 3.5-kb RNA are within in-frame splice donor and acceptor sites suggests strongly that the 3.5-kb RNA is derived from the 4.0-kb RNA by a temperature-sensitive splice mechanism. Data presented here show unequivocally that formation of the 3.5-kb MuSV ts110 RNA from which the P85gag-mos polypeptide is translated is temperature sensitive. At 33 degrees C, with S1 analysis, the 3.5-kb RNA is found readily in 6m2 cells. Within 4 h of a shift to 39 degrees C, however, only trace amounts of this RNA can be found. Moreover, reshifting 6m2 cells to 33 degrees C permits the reappearance of the 3.5-kb RNA at its original level.
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PMID:S1 nuclease mapping of viral RNAs from a temperature-sensitive transformation mutant of murine sarcoma virus. 632 48