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

In an RNase III-deficient mutant of Escherichia coli, all 23 S ribosomal RNA in ribosomes is present in an unprocessed form with a double-stranded stem at the base of the molecule stable enough to be detected by electron microscopy under conditions where all other secondary structure is denatured. Molecules with variable stem lengths enter freely into polysomes, consistent with the existence of a similar but much shorter stem in mature 23 S rRNA in wild-type ribosomes.
J Mol Biol 1985 Dec 05
PMID:Why is processing of 23 S ribosomal RNA in Escherichia coli not obligate for its function? 391 11

Infection of RNase III- (rnc) Escherichia coli cells with bacteriophage T4 delta 27, a deletion mutant missing seven out of the ten genes in the tRNA transcription unit, results in the accumulation of a tRNA precursor (10.5-S RNA) that contains the sequences of tRNAGln, tRNALeu and species 1 RNA [Pragai and Apirion (1981) J. Mol. Biol. 153, 619-630]. In vitro studies, using partially purified RNase III or cell extracts and 10.5-S RNA as substrate, have revealed a cleavage site at the 5' side of the molecule. A computerized secondary structure suggests that the RNase III cleavage site can be placed in a small bulge which could be part of a duplex structure and is adjacent to A-A-G and its complementary sequence U-U-U in the same relative relationships found for most RNase III cleavage sites were the adjacent sequences are (A-A-G/U-U-C). Under normal processing conditions (presence of RNase III) the 3' end of the processed intermediate precursors, 10.1-S and p2Sp1 RNAs, is C-U-U-(U1-2)-UOH, which is determined by a stem and loop structure that could serve as a rho-independent termination signal site. However, in the absence of RNase III, the accumulated 10.5-S precursor RNA does not terminate at the same site and its 3' end is shifted a few nucleotides downstream. Thus, RNase III, besides playing a role in processing of 10.5-S RNA, also affects the termination of that molecule, even though both sites, the RNase III cleavage site and the termination site, are about 390 nucleotides apart.
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PMID:The ribonuclease-III-processing site near the 5' end of an RNA precursor of bacteriophage T4 and its effect on termination. 397 89

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

The int gene of phage lambda encodes a protein involved in site-specific recombination. Its expression is regulated differentially during successive phases of the lambda infective cycle. The gene is transcribed early after infection from one promoter, pL, and later from a second promoter pI. Each transcription event requires different positive activation factors, lambda N and cII proteins, respectively. Transcription from the pI promoter, located adjacent to int, passes through int and terminates 277 nucleotides beyond int at tI. Polymerases initiating at pL transcribe through tI and into the b segment of lambda DNA. The read-through pL transcript is sensitive to cleavage by the endonuclease, RNase III, both in vivo and in vitro. Two specific cuts are made by RNase III in a double-stranded structure about 260 nucleotides beyond int in the location of the tI terminator. Functionally, the processed pL transcript is unable to synthesize the int gene product, whereas the terminated and unprocessed pI transcript expresses int. Interestingly, unprocessed pL transcripts made in hosts defective in RNase III (rnc-) can express int. Thus a correlation exists between processing and negative control of int expression. The place where processing occurs, some 260 nucleotides beyond int, is called sib, and the control of int expression from this site is called retroregulation. Retroregulation by sib is not restricted just to the int gene; we show that if the sib site is cloned beyond a bacterial gene, the gene is controlled by sib and RNase III. Specific models are discussed with respect to control of gene expression by RNase III from a site beyond the controlled gene.
J Mol Biol 1984 Jun 15
PMID:Removal of a terminator structure by RNA processing regulates int gene expression. 623

The lambda int gene product, integrase, recombines phage and bacterial DNA at a specific site during the integration step of lysogeny. Regulation of integrase synthesis is complex. (1) Transcription of the gene can occur from either of two promoters. lambda cII protein activates transcription initiation near int at pI. The lambda N protein allows transcription of int from pL. N protein acts by preventing transcription termination at several terminators between pL and int. (2) The expression of integrase is also subject to post-transcriptional regulation by a site, sib, which is located beyond int in the b region of lambda. Expression of int from pL is inhibited by sib, whereas that from pI is not. The negative control of int expression by sib is termed retroregulation. Retroregulation of int is caused, in part, by processing of the pL transcript at the sib site by RNase III of Escherichia coli. The exonuclease, Bal31, was used to generate a set of deletions to define the sib regulatory site. Both sib+ and sib- deletions were sequenced, and it was concluded from this and other work that a dyad symmetry present in the b region, 270 base-pairs from int, was necessary for retroregulation. The RNA structure of this segment is similar to other RNase III-sensitive sites found in E. coli and phage RNAs.
J Mol Biol 1983 May 15
PMID:Deletion analysis of the retroregulatory site for the lambda int gene. 630 22

The DNA sequences of three major class III T3 RNA polymerase promoters located at 45.0, 55.0, and 64.8% on the standard T3 genetic map have been determined. The precise RNA initiation sites were also determined by 5'-terminal RNA sequence analysis of the transcripts synthesized from the promoter-containing DNA fragments. Alignment of these three class III promoters and a previously determined T3 RNA polymerase promoter at 1.05% on T3 genetic map, with start points of transcription (+1) in register, indicates a high degree of sequence conservation among the four T3 RNA polymerase promoters. The sequences are identical between positions -12 and +4 and are uniformly A-T between -12 and -17. The conserved portion of the (-) strand sequence is 5' (sequence in text) Upstream from -17 and downstream from +4 the sequences diverge. Comparison of this sequence with a prototype 23-base pair promoter sequence for T7 RNA polymerase shows overall homology between positions -17 and +4 with conserved divergence at residues -2 and between -10 and -12. Furthermore, careful examination of the nucleotide sequences around 45.0 and 64.8 T3 map units shows that the putative RNA sequences arising from these regions by overlapping transcription from upstream promoters can be arranged into stable stemloop structures thought to be required for RNase III cleavage. This pattern is similar to those reported for the corresponding T7 RNA polymerase promoters on T7 DNA (Dunn. J. J., and Studier, F. W. (1983) J. Mol. Biol. 166, 477-535).
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PMID:Locations and nucleotide sequences of three major class III promoters for bacteriophage T3 RNA polymerase on T3 DNA. 631 18

We have previously demonstrated a highly significant relationship between incorporation of 5-fluorouracil (FUra) into total cellular RNA and loss of clonogenic survival. The present study extends these findings by demonstrating a similar relationship between incorporation of FUra into preribosomal nuclear RNA (45 S and 32 S) and lethal cellular events. The results also demonstrate that the extent of FUra incorporation into preribosomal RNA (prRNA) correlates significantly with inhibition of maturation to cytoplasmic 28 S and 18 S rRNA. These findings suggest that the incorporation of FUra into prRNA alters recognition sites involved in the processing of 45 S and 32 S RNA. These data are further supported by our finding of an enhanced degradation of (FUra)prRNA by RNase III, an enzyme implicated in the maturation of Escherichia coli prRNA and T7 mRNA. These observations suggest that the incorporation of FUra into prRNA is responsible for altered processing to cytoplasmic rRNA and cell lethality.
Mol Pharmacol 1984 Jul
PMID:Lethality associated with incorporation of 5-fluorouracil into preribosomal RNA. 656 75

We studied the distribution of repetitive sequence elements capable of forming double-stranded regions in nuclear RNA of HeLa, KB, and L cells. In human RNA populations, we called these regions duplex Alu family RNA (dAfRNA) because they represent transcripts of the highly reiterated family of DNA regions known as "Alu family DNA" (Rubin et al., Nature (London) 284:372-374, 1980). Although the dAfRNA populations of both human cell lines (HeLa and KB) have low sequence complexity, they represent 5% of the total heterogeneous nuclear RNA and have identical fingerprints; mouse L-cell dAf-like RNA (which has a similar complexity) represents only 2% of the total heterogeneous nuclear RNA and has an entirely different fingerprint. We utilized Escherichia coli RNase III as a highly specific reagent for the recognition of RNA:RNA duplex structure. This enzyme cleaves within the six characteristic RNase T1-resistant oligonucleotides of HeLa- and KB-cell dAfRNA (Robertson et al., J. Mol. Biol. 115:571-589, 1977). In addition, the size of heterogeneous nuclear RNA from all three cell types is reduced from greater than 32S to about 15S after RNase III treatment. We conclude that this size shift is a result of cleavage within dAfRNA regions and that such regions are present in most or all of the large RNA transcripts of these cells.
Mol Cell Biol 1984 Feb
PMID:Structure and distribution of Alu family sequences or their analogs within heterogeneous nuclear RNA of HeLa, KB, and L cells. 670 May 93

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


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