Removal of a terminator structure by RNA processing regulates int gene expression

Schmeissner, Ursula; McKenney, Keith; Rosenberg, Martin; Court, Donald L.

doi:10.1016/0022-2836(84)90381-4

Cited by 137 publications

(76 citation statements)

References 22 publications

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“…RNase III can control mRNA translational efficiencies, and RNA physical and functional halflives. Current evidence indicates that RNase HI-catalyzed cleavage can remove RNA sequences which would otherwise impede productive binding of mRNA to the 30S ribosomal subunit, or block the action of degradative ribonucleases [8][9][10]. RNase IH may also control translation initiation by acting as an mRNA-binding protein [ 1 1 ].…”

Section: Introductionmentioning

confidence: 99%

Ribonuclease III cleavage of a bacteriophage T7 processing signal. Divalent cation specificity, and specific anion effects

Chelladurai

Zhang

et al. 1993

Nucl Acids Res

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Section: Introductionmentioning

confidence: 99%

Ribonuclease III cleavage of a bacteriophage T7 processing signal. Divalent cation specificity, and specific anion effects

Chelladurai

Zhang

et al. 1993

Nucl Acids Res

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“…Their processive action is impeded by secondary structures as, for example, a stem-loop structure at the 3' end of a transcript (Newbury et al 1987;Plamann and Stauffer 1990). Endonucleases can remove such secondary structures and thus generate new 3' ends that are susceptible to further exonucleolytic degradation (Schmeissner et al 1984;Regnier and Hajnsdorf 1991). At least in some cases, an endonucleolytic cleavage triggers the decay of the message.…”

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confidence: 99%

“…At least in some cases, an endonucleolytic cleavage triggers the decay of the message. Endoribonuclease RNase III is known to initiate the decay of a few specific mRNAs (Schmeissner et al 1984;Portier et al 1987;Bardwell et al 1989;Regnier and Grunberg-Manago 1989). Other endonuclease activities have been described that are believed to be involved in the degradation of specific mRNAs (Cannistraro and Kennel 1989;Lundberg et al 1990), but their role in globPtesent addresses: 'The Salk Institute for Biological Studies, San Diego, California 92186-5800; ^Centre de Recherche de Biochimie et Genetique Cellulaire du Centre National de la Recherche Scientifique, 31062 Toulouse, France.…”

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confidence: 99%

Specificity of Escherichia coli endoribonuclease RNase E: in vivo and in vitro analysis of mutants in a bacteriophage T4 mRNA processing site.

Ehretsmann¹,

Carpousis²,

Krisch³

1992

Genes Dev.

209

147

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Endoribonuclease RNase £ has an important role in the processing and degradation of bacteriophage T4 and Escherichia coli mRNAs. We have undertaken a mutational analysis of the -71 RNase E processing site of T4 gene 32. A Series of mutations were introduced into a synthetic T4 sequence cloned on a plasmid, and their effects on processing were analyzed in vivo. The same mutations were transferred into T4 by homologous recombination. In both the plasmid and the phage contexts the processing of the transcripts was similarly affected by the mutations. Partially purified RNase E has also been used to ascertain the effect of these mutations on RNase E processing in vitro. The hierarchy of the efficiency of processing of the various mutant transcripts was the same in vivo and in vitro. These results and an analysis of all of the known putative RNase E sites suggest a consensus sequence RAUUW (R = A or G; W ^ A or U) at the cleavage site. Modifications of the stem-loop structure downstream of the -71 site indicate that a secondary structure is required for RNase E processing. Processing by RNase E was apparently inhibited by sequences that sequester the site in secondary structure.

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“…The enzyme is involved in the processing of mRNA from bacteriophage T4 genes 32 and 59 in vivo. Processing of these messages resulted in destabilization of the portion of the mRNA upstream of the cleavage site (Mudd et al 1988;Carpousis et al 1989) and thus may have a role in retroregulation (Schmeissner et al 1984) of upstream gene expression. A comparison of the cleavage sites found in the noncoding RNAs and the T4 mRNAs revealed similarities in sequence at the cleavage sites and in the potential to form RNA secondary structure just downstream of the sites (Tomcs~inyi and Apirion 1985;Mudd et al 1988;Carpousis et al 1989).…”

mentioning

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Escherichia coli RNase E has a role in the decay of bacteriophage T4 mRNA.

Mudd¹,

Carpousis²,

Krisch³

1990

Genes Dev.

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Bacteriophage T4 mRNAs are markedly stabilized, both chemically and functionally, in an Escherichia coli strain deficient in the RNA-processing endonuclease RNase E. The functional stability of total T4 messages increased 6-fold; we were unable to detect a T4 message whose functional stability was not increased. There was a 4-fold increase in the chemical stability of total T4 RNA. The degree of chemical stabilization of six specific T4 mRNAs examined varied from a maximum of 28-fold to a minimum of 1.5-fold. In the RNase Edeficient strain, several minutes delay and a slower rate of progeny production led to a reduction in final phage yield of -50%. Although the effect of the rne temperature-sensitive mutation could be indirect, the simplest interpretation of our results is that RNase E acts directly in the degradation of many T4 mRNAs.[Key Words: Bacteriophage T4; mRNA decay; mRNA processing; mRNA stability; ribonuclease El Received September 13, 1989; revised version accepted February 7, 1990.Escherichia coli RNase E is an endoribonuclease that has been shown to process 9S RNA to a precursor of 5S rRNA (Ghora and Apirion 1978) and also to process RNA1, the inhibitor of ColE1 plasmid replication (Tomcs~inyi and Apirion 1985) both in vitro and in vivo. RNase E did not appear to have a general role in mRNA decay in E. coli (Apirion and Gitelman 1980}, although the synthesis of some E. coli proteins was affected by the mutation (Gitelman and Apirion 1980). The enzyme is involved in the processing of mRNA from bacteriophage T4 genes 32 and 59 in vivo. Processing of these messages resulted in destabilization of the portion of the mRNA upstream of the cleavage site (Mudd et al. 1988;Carpousis et al. 1989) and thus may have a role in retroregulation (Schmeissner et al. 1984) of upstream gene expression. A comparison of the cleavage sites found in the noncoding RNAs and the T4 mRNAs revealed similarities in sequence at the cleavage sites and in the potential to form RNA secondary structure just downstream of the sites (Tomcs~inyi and Apirion 1985;Mudd et al. 1988;Carpousis et al. 1989).As yet, the nucleases that determine the rate of functional decay of total mRNA in E. coil or its phage have not been identified. A mutation in the E. coli ams gene was found to have a five-to sixfold effect on the chemical stability of total E. coli RNAs, but it did not affect functional stability significantly (Kuwano et al. 1977;Ono and Kuwano 1979). E. coli RNases III (see Portier et al. 1987), E (Mudd et al. 1988;Carpousis et al. 1989), and other as yet unidentified endonucleases (Cannistraro et al. 1986; Baga et al. 1988; Melefors and von Gabain 1988; Uzan et al. 1988) have been implicated in the decay of a few specific bacterial or phage mRNAs. In this paper we present evidence suggesting that E. coli RNase E has a major role in the functional and chemical decay of many bacteriophage T4 mRNAs. Results E. coli RNase E affects the functional stability of T4 mRNAsThe functional stability of mRNA can be estimated from the ability of t...

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Removal of a terminator structure by RNA processing regulates int gene expression

Cited by 137 publications

References 22 publications

Ribonuclease III cleavage of a bacteriophage T7 processing signal. Divalent cation specificity, and specific anion effects

Ribonuclease III cleavage of a bacteriophage T7 processing signal. Divalent cation specificity, and specific anion effects

Specificity of Escherichia coli endoribonuclease RNase E: in vivo and in vitro analysis of mutants in a bacteriophage T4 mRNA processing site.

Escherichia coli RNase E has a role in the decay of bacteriophage T4 mRNA.

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