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)

We have isolated and characterized a nuclear gene, MSS18, which is implicated in the splicing of intron aI5 beta of the mitochondrial cox1 transcript (subunit 1 of the cytochrome c oxidase). Northern blotting and S1 nuclease protection experiments as well as the analysis of mitochondrial point revertants suggest that mss18 mutations block (perhaps indirectly) the cleavage of the 5' exon-intron junction of aI5 beta. Mitochondrial point revertants also indicate that up to 13 bases of the aI5 beta exon sequence, upstream of the 5' splice site of aI5 beta, are involved in vivo in the splicing of this intron. The implications of this result on the splicing of group I introns are discussed.
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PMID:MSS18, a yeast nuclear gene involved in the splicing of intron aI5 beta of the mitochondrial cox1 transcript. 284 50

The product of the yeast nuclear gene PET494 is required specifically for the translation of the mitochondrially encoded subunit III of cytochrome c oxidase. We have determined the DNA sequence of a 1.9 kb fragment carrying PET494. The sequence contains a single long open reading frame of 489 codons. This open reading frame encodes the PET494 protein since the DNA sequence of the corresponding fragment derived from a strain with a known pet494 amber mutation contained an in frame UAG codon. The results of S1 nuclease protection experiments demonstrated that this region is transcribed and that the 5' ends of the major transcripts lie 30 to 40 base-pairs upstream of the first AUG codon in the PET494 reading frame. The predicted PET494 protein has a highly basic amino-terminal domain of 66 amino acids followed by a stretch of 32 uncharged residues, half of which are hydrophobic. The remainder of the protein is not unusual in amino acid composition or distribution except that the carboxyterminal region is notably basic. The phenotype of mutations generated in vitro around codon 119 by exonuclease digestion and linker insertion indicated that this region is dispensable for function. A mutation caused by deletion of 101 bp of coding sequence behaved like a simple frameshift when inserted into the chromosome: it was partially suppressed by the recessive non-group specific frameshift suppressor suf13 and reverted to Pet+ phenotype by mutations linked to PET494.
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PMID:Primary structure of wild-type and mutant alleles of the PET494 gene of Saccharomyces cerevisiae. 301 52

In Saccharomyces cerevisiae, the mitochondrial gene encoding the subunit I of cytochrome c oxidase (oxi-3 gene) is interrupted by intervening sequences. In this report, a nuclear mutation [referred to as mss51 in Faye, G. & Simon, M. (1983) Cell 32, 77-87] that specifically affects the processing of oxi-3 pre-mRNA was further characterized. DNA probes covering each oxi-3 exon-intron boundary were individually hybridized to wild-type and mutant mitochondrial RNA. By a technique relying on the S1 nuclease resistance or sensitivity of the RNA X DNA hybrids thereof, we have shown which site needs the MSS51 gene product to be cleaved. The mutation in the MSS51 gene gave rise to a complex pattern of splicing: the third intron was excised efficiently but the first two introns remained bracketed by their flanking exons. Further, the fourth and fifth introns were only partially split from their common exon and remained fused to their upstream and downstream flanking exon, respectively. Several plausible roles for the MSS51 gene product are discussed.
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PMID:Steps in processing of the mitochondrial cytochrome oxidase subunit I pre-mRNA affected by a nuclear mutation in yeast. 632 Jan 75

We analyzed expression elements of three disparate groups of mitochondrial genes in Neurospora crassa, apocytochrome b (COB), cytochrome c oxidase 1 (COX1), and the clustered ATP8-ATP6-mtATP9-COX2. To identify promoter sequences we employed the published N. crassa consensus sequence for COB and rRNA genes, and we found closely related sequences within the 5'-regions of both COX1 and the ATP8-COX2 transcriptional units. We determined that the mature COX1 RNA includes two flanking unassigned reading frame (URF) sequences, but the 3'-flanking ND1 is not included in the COX1 mRNA. The ATP8-ATP6-mtATP9-COX2 polycistronic transcript does not include an adjacent 5'-URF sequence. Primer extension analysis showed one likely 5'-end for the COX1 transcript, which is 73 nucleotides downstream of the consensus promoter sequence and is the first nucleotide 3' of the sequence for the tRNA(cys). Primer extension analysis and S1 nuclease mapping of the ATP8-COX2 RNA showed that the 5'-end for this transcript is the first nucleotide 3' of the consensus promoter sequence. We performed gel-shift experiments to detect proteins in mitochondria that bind to transcripts as possible regulatory proteins. The 5'-untranslated region (UTR) RNAs of COB, COX1, and ATP8-COX2 appear to bind both unique proteins and an overlapping group of two to four proteins of approximately 155-45 M(r). We successively deleted regions of the RNA 5'-UTRs to identify sequences that bound these proteins. Similar predicted stem-loop secondary structures were detected in the protein-binding regions of all three UTRs.
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PMID:Transcripts and transcript-binding proteins in mitochondria of Neurospora crassa. 1612 Mar 32