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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The transcription of the gltX gene encoding the glutamyl-tRNA synthetase and of the adjacent valU and alaW tRNA operons of Escherichia coli K-12 has been studied. The alaW operon containing two tRNA(GGCAla) genes, is 800 base-pairs downstream from the gltX terminator and is transcribed from the same strand. The valU operon, containing three tRNA(UACVal) and one tRNA(UUULys) (the wild-type allele of supN) genes, is adjacent to gltX and is transcribed from the opposite strand. Its only promoter is upstream from the gltX promoters. The gltX gene transcript is monocistronic and its transcription initiates at three promoters, P1, P2 and P3. The transcripts from one or more of these promoters are processed by RNase E to generate two major species of gltX mRNA, which are stable and whose relative abundance varies with growth conditions. The stability of gltX mRNA decreases in an RNase E- strain and its level increases with growth rate about three times more than that of the glutamyl-tRNA synthetase. The 5' region of these mRNAs can adopt a stable secondary structure (close to the ribosome binding site) that is similar to the anticodon and part of the dihydroU stems and loops of tRNA(Glu), and which might be involved in translational regulation of GluRS synthesis. The gltX and valU promoters share the same AT-rich and bent upstream region, whose position coincides with the position of the upstream activating sequences of tRNA and rRNA promoters to which they are similar. This suggests that gltX and valU share transcriptional regulatory mechanisms.
J Mol Biol 1990 Aug 20
PMID:Closely spaced and divergent promoters for an aminoacyl-tRNA synthetase gene and a tRNA operon in Escherichia coli. Transcriptional and post-transcriptional regulation of gltX, valU and alaW. 220 77

Strains carrying plasmids that code for 10Sa RNA synthesize a larger molecule when the RNA processing enzyme RNase E is inactivated. The T1 fingerprint of 10Sa RNA and the larger molecule is very similar, but the latter contains additional oligonucleotides. We show that the larger RNA is converted to the smaller, mature RNA. The precursor molecule starts with an adenosine triphosphate and is therefore a primary transcript. RNase E is not the enzyme that processes p10Sa (precursor 10Sa) RNA into 10Sa RNA. The cell extract contains an activity that carries out this conversion. This activity requires the dication Mn2+.
Mol Gen Genet 1989 Jun
PMID:A precursor for a small stable RNA (10Sa RNA) of Escherichia coli. 247 57

Stability of RNA was tested in strains of Escherichia coli carrying single, double, or triple mutations in the RNA processing enzymes RNase III, RNase E and RNase P. Tests were carried out for total pulse labeled RNA, beta-galactosidase mRNA and for the decay of preexisting RNA during carbon starvation. Decay of RNA was measured at permissive and nonpermissive temperatures, and in no case were significant differences between mutants and non-mutant strains found. Therefore, we conclude that the three processing enzymes; RNase III, E and P do not contribute significantly to turnover of RNA IN Escherichia coli.
Mol Gen Genet 1980 Jan
PMID:Decay of RNA in RNA processing mutants of Escherichia coli. 615 28

Transformation of an RNA-processing mutant (rne, RNase E-) of Escherichia coli with a recombinant plasmid containing the promoter region of the ribosomal cluster rrnA and portions from the 3' region of the rrnD cluster results in the accumulation of the precursors to 5 S ribosomal RNAs at the permissive as well as that of two full-length transcripts and a processing intermediate at the nonpermissive temperature. The two full-length transcripts start from the two rrnA promoters, which are about 120 nucleotides apart. This plasmid, pJR3 delta, contains an intact 5 S rRNA gene and portions from the 16 S and 23 S rRNA genes. Analysis of the major plasmid-specific RNA species revealed that RNA molecules initiated in vivo from the first promoter (P1) start with pppA, while transcripts from the second promoter (P2) contain either pppG or pppC at their 5' ends. Termination occurs mainly at the first available termination site. Full-length transcripts initiated from both promoters are processed to precursors of 5 S rRNAs in vivo at the permissive temperature, but only about 20% of these transcripts are processed to mature 5 S rRNA. RNA1 and RNA2 (the transcripts initiated from P1 and P2, respectively) and RNA3 (an RNA-processing intermediate containing the entire 5 S region and the 3' end of the transcripts) can be cleaved in vitro by cell extracts of wild type strains resulting in precursor and mature 5 S rRNAs in a reaction that is RNase E dependent but not ribosome dependent. The 5' end of the processed 5 S rRNA can correspond to the 5' end of mature 5 S rRNA or it can contain one to three additional nucleotides.
J Mol Biol 1983 Aug 15
PMID:Initiation, processing and termination of ribosomal RNA from a hybrid 5 S ribosomal RNA gene in a plasmid. 619 78

An RNA encompassing the 3' 147 residues of the mRNA for ribosomal protein S20 in Escherichia coli constitutes a naturally occurring degradative intermediate whose formation depends on RNase E. We have investigated the role of internal stem-loop structures in the RNase E-dependent cleavage which generates this product from S20 mRNA in a partially fractionated processing system in vitro. Individual stem-loops have been removed by deletion or destabilized by point mutations. No single hairpin structure is absolutely required for RNase E-dependent cleavage at the site 147 residues from the 3' end of the RNA. Primary sequences or secondary structures 5' or 3' to this site exert only a modest influence on the specificity of cleavage but can strongly modify its rate. Moreover, mutations in the S20 mRNA which destabilize stems 5' or 3' to the prominent cleavage site also reveal several strong cryptic RNase E cleavage sites. These data greatly strengthen the hypothesis that RNase E is a single-strand specific endoribonuclease. Our data further demonstrate that stem-loop structures adjacent to the prominent cleavage site are unlikely to provide a site of recognition for RNase E. Rather, they appear to stabilize (or "anchor") the local secondary structure so that the cleavage site is single-stranded and to occlude alternative sites so that the initial products of cleavage resist further attack.
J Mol Biol 1993 Dec 20
PMID:The role of RNA structure in determining RNase E-dependent cleavage sites in the mRNA for ribosomal protein S20 in vitro. 750 37

The two cleavages made by RNase III in the transcripts of the pnp gene of Escherichia coli, 80 nucleotides upstream of the coding sequence of polynucleotide phosphorylase, were previously demonstrated to trigger the rapid degradation of the pnp messenger. In this paper, we demonstrate that the 5' end of the RNase III processed pnp mRNA is attacked by ribonucleases more efficiently than the rest of the molecule. Several 5' extremities resulting from cleavages occurring in the first 500 nucleotides of the pnp transcript have been identified. Three of them referred to as X, Y and W occur in the wild-type strain at the beginning of the coding sequence of the pnp mRNA. The mRNA appears to be cleaved more efficiently at the X site, proximal to the initiation codon, than at sites Y and W located downstream. In vitro, the maturation at X is catalysed by RNase E but not by RNase III. Accumulation of RNA processed at X in RNase E deficient strains leads us to postulate that X is a high affinity primary site which is slowly cleaved by the residual activity of thermosensitive RNase E at non-permissive temperature and that secondary sites located downstream are processed less efficiently than X. Taken together, our results suggest that in wild-type E. coli the degradation of the RNase III processed mRNA is mediated by RNase E.
J Mol Biol 1994 Jun 17
PMID:Nucleolytic inactivation and degradation of the RNase III processed pnp message encoding polynucleotide phosphorylase of Escherichia coli. 751 38

Transiently stable products derived from the endonuclease cleavage of transcripts from the secEnusG and rplKAJLrpoBC operons have been identified. Cleavage sites for RNase III occur in the leader of the secEnusG transcript and in the L12-beta intercistronic space of the rplKAJLrpoBC transcript. A single RNase E cleavage site was located in the L1-L10 intergenic space. Inactivation of RNase III and RNase E results respectively in a one- to twofold and a greater than 10-fold stabilization of five mRNA sequences from within the secE, nusG, L11-L1, L10 and beta encoding cistrons. The relative amounts of each of these five mRNA sequences were found to be nearly constant when measured either in the presence or absence of cleavage by RNase III or RNase E. This clearly implies that any increases in the stability of these mRNA sequences resulting from the inactivation of processing by RNase III or RNAase E are counterbalanced by changes in the mRNA synthesis rates. The mechanism that links mRNA synthesis to mRNA decay is not known.
Mol Microbiol 1994 Mar
PMID:Coupling between mRNA synthesis and mRNA stability in Escherichia coli. 751 86

We have identified an mRNA element that is involved in the initial cleavage of the pufBALMX mRNA species in Rhodobacter capsulatus. This endoribonuclease recognition site, the first to be identified in a bacterial species other than Escherichia coli, shows strong similarities to mRNA sequences cleaved by the endoribonuclease E in E. coli. The presence of an RNase E-like enzyme in R. capsulatus is further supported by in vitro cleavage of E. coli transcripts by R. capsulatus extracts at sites attributed to RNase E and by the cross-reaction of a polypeptide from R. capsulatus with antisera against E. coli RNase E. Our data provide evidence that mRNAs are degraded in different bacterial species by enzymes with similar recognition sequences and activities. We present a model that attributes the segmental differences in stability of the polycistronic puf transcript to a specific distribution of mRNA decay-promoting and mRNA decay-impeding elements.
Mol Microbiol 1995 Mar
PMID:Identification of an mRNA element promoting rate-limiting cleavage of the polycistronic puf mRNA in Rhodobacter capsulatus by an enzyme similar to RNase E. 754 24

The 20S proteasome (prosome) is a highly organized multi-protein complex with approximate molecular weight of about 700 kDa. Whilst the role of the proteasome in the processing and turnover of cellular proteins is becoming clearer, its relationship with RNA remains obscure. Over the last decade the possibility of association of proteasomes with specific RNAs or mRNPs have been particularly controversial. Proteasomes were reported to inhibit translation of viral mRNAs and to be tightly associated with RNase activity. It is possible that proteasomes are also involved in cellular RNA breakdown and RNA processing like prokaryotic RNase E.
Mol Biol Rep 1995
PMID:Relationships between proteasomes and RNA. 756 63

mRNA degradation in Escherichia coli is mediated by a combination of exo- and endoribonucleases. We present evidence for a multiprotein complex which includes at least two enzymes that play important roles in mRNA degradation: the exoribonuclease polynucleotide phosphorylase (PNPase) and the endoribonuclease RNase E. An activity which impedes the processive activity of PNPase at stem-loop structures also appears to be associated with the complex. This complex is estimated to have a molecular mass of about 500 kDa and includes several additional polypeptides whose functions are unknown. The identification of a complex which includes several activities associated with mRNA degradation has implications for the mechanisms and co-ordinated control of mRNA degradation.
Mol Microbiol 1994 Nov
PMID:A protein complex mediating mRNA degradation in Escherichia coli. 789 59


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