mRNA degradation in procaryotes

Ehretsmann, C P; Carpousis, Agamemnon J.; Krisch, Henry

doi:10.1096/fasebj.6.13.1397840

Cited by 91 publications

(62 citation statements)

References 1 publication

(1 reference statement)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The N-terminal half (NTH) 1 of RNaseE is sufficient for basal catalytic activity (10) that is able to support cell viability (11). The RNaseE-catalyzed hydrolysis of RNA in vivo is influenced by the C-terminal half (12)(13)(14), which contains an arginine-rich RNA-binding domain (10, 14 -17) and several sites (18,19) that serve in the assembly of the E. coli RNA degradosome (for reviews, see Refs.…”

Section: Panel A)mentioning

confidence: 99%

“…The mechanism by which the b site within the context of a 9 S transcript is cleaved by RNaseE despite the absence of an upstream G remains to be determined. It is possible that the recruitment of RNaseE is regulated by some secondary structural element(s) (17) as suggested relatively early in the study of RNaseE (1,30) or the distance between susceptible sequences and a monophosphate at the 5Ј end (25). From the above, it can be seen that an understanding of the recognition and hydrolysis of RNA by RNaseE will require a systematic analysis of the contribution of RNA sequence and structure, including the phosphorylation status at the 5Ј end, the multiple domains within the C-terminal half of RNaseE, and the effects of other degradosome component.…”

Section: Panel A)mentioning

confidence: 99%

“…RNaseE is a single-stranded-specific endoribonuclease (1)(2)(3) that is required for the rapid decay of many if not most transcripts in Escherichia coli (for reviews, see Refs. 4 -6) and the correct processing of precursors of, for example, ribosomal and transfer RNAs (7,8).…”

mentioning

confidence: 99%

See 2 more Smart Citations

Determination of the Catalytic Parameters of the N-terminal Half of Escherichia coli Ribonuclease E and the Identification of Critical Functional Groups in RNA Substrates

Redko

Tock

Adams

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

Ribonuclease E is required for the rapid decay and correct processing of RNA in Escherichia coli. A detailed understanding of the hydrolysis of RNA by this and related enzymes will require the integration of structural and molecular data with quantitative measurements of RNA hydrolysis. Therefore, an assay for RNaseE that can be set up to have relatively high throughput while being sensitive and quantitative will be advantageous. Here we describe such an assay, which is based on the automated high pressure liquid chromatography analysis of fluorescently labeled RNA samples. We have used this assay to optimize reaction conditions, to determine for the first time the catalytic parameters for a polypeptide of RNaseE, and to investigate the RNaseE-catalyzed reaction through the modification of functional groups within an RNA substrate. We find that catalysis is dependent on both protonated and unprotonated functional groups and that the recognition of a guanosine sequence determinant that is upstream of the scissile bond appears to consist of interactions with the exocyclic 2-amino group, the 7N of the nucleobase and the imino proton or 6-keto group. Additionally, we find that a ribose-like sugar conformation is preferred in the 5 -nucleotide of the scissile phosphodiester bond and that a 2 -hydroxyl group proton is not essential. Steric bulk at the 2 position in the 5 -nucleotide appears to be inhibitory to the reaction. Combined, these observations establish a foundation for the functional interpretation of a three-dimensional structure of the catalytic domain of RNaseE when solved.RNaseE is a single-stranded-specific endoribonuclease (1-3) that is required for the rapid decay of many if not most transcripts in Escherichia coli (for reviews, see Refs. 4 -6) and the correct processing of precursors of, for example, ribosomal and transfer RNAs (7,8). RNaseE generates products terminating in a 3Ј-hydroxyl and a 5Ј-phosphate (9) indicating that the reaction involves the attack of water on the susceptible phosphodiester bond followed by scission of 3Ј-oxygen-phosphorus bond. The RNaseE polypeptide consists of 1061 residues (Fig.

show abstract

Section: Panel A)mentioning

confidence: 99%

Section: Panel A)mentioning

confidence: 99%

See 1 more Smart Citation

Determination of the Catalytic Parameters of the N-terminal Half of Escherichia coli Ribonuclease E and the Identification of Critical Functional Groups in RNA Substrates

Redko

Tock

Adams

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Ribonuclease E (RNase E), which was discovered initially in Escherichia coli as a ribosomal-RNA-processing enzyme, has since been found to have an important role in the degradation of a variety of E. coli messenger RNAs (for earlier reviews, see Melefors et a/., 1993;Ehretsmann et a/., 1992a) and, by its action on RNAl (Tomcsanyi and Apirion, 1985), the antisense regulator of replication of ColEl-type plasmids, also to be able to regulate DNA synthesis (Lin-Chao and Cohen, 1991). Although a mutation affecting RNase E activity was identified almost 20 years ago, and the ribonucleolytic activity of the RNase E protein was demonstrated soon afterwards, RNase E remains a 'wonderfully mysterious enzyme', as it was termed by an anonymous reviewer of a research proposal submitted by one of us (S.N.C.)…”

Section: Introductionmentioning

confidence: 99%

RNase E: still a wonderfully mysterious enzyme

Cohen

McDowall

1997

Molecular Microbiology

130

106

View full text Add to dashboard Cite

SummaryRibonuclease E (RNase E), which is encoded by an essential Escherichia coli gene known variously as me, ams, and hmp, was discovered initially as an rRNA-processing enzyme but is now known to have a general role in RNA decay. Multiple functions, including the ability t o cleave RNA endonucleolytically in AU-rich single-strand regions, RNA-binding capabilities, and the ability to interact with polynucleotide phosphorylase and other proteins implicated in the processing and degradation of RNA, are encoded by its 1061 amino acid residues. The presence of homologues and functional analogues of the m e gene in a variety of prokaryotic and eukaryotic species suggests that its functions have been highly conserved during evolution. While much has been learned in recent years about the structure and functions of RNase E, there is continuing mystery about possible additional activities and molecular interactions of this enzyme.

show abstract

“…RNase E is an E. coli endoribonuclease that has been shown to have a key role in the processing of ribosomal RNA and the degradation of a variety of messenger RNAs; additionally, by its cleavage of RNA I, the antisense repressor of replication of ColE1-type plasmids, RNase E can regulate DNA replication (for reviews, see Ehretsmann et al, 1992;Melefors et al, 1993;Cohen and McDowall, 1997). This enzyme is a 118 kDa, 1061 amino acid protein that cleaves single-stranded regions of RNA site specifically in segments rich in A þ U nucleotides; in E. coli cells, RNase E can form macromolecular complexes with other proteins that assist in, or otherwise affect, RNA decay (for a recent review, see Cohen and McDowall, 1997).…”

Section: Introductionmentioning

confidence: 99%

A developmentally regulated Streptomyces endoribonuclease resembles ribonuclease E of Escherichia coli

Hagège

Cohen

1997

Molecular Microbiology

View full text Add to dashboard Cite

SummaryWe report that the Streptomyces species S. lividans and S. coelicolor, morphologically complex Grampositive soil bacteria, contain a developmentally regulated endoribonuclease activity (here named RNase ES) that functionally and immunologically resembles Escherichia coli RNase E. In Streptomyces cells, RNA I -the antisense repressor of replication of ColE1-type plasmids -is cleaved at sites attacked by RNase E. A Mg 2þ -dependent endonuclease that produces RNase E-like cleavages in RNA I and 9S ribosomal RNA was identified in S. lividans cell extracts. A Streptomyces peptide migrating at 70 kDa in SDS/polyacrylamide gels binds to RNase E substrates and reacts with three separate anti-RNase E monoclonal antibodies; the endonucleolytic cleavage activity co-purified with the immunoreactive 70 kDa peptide. We show that RNase ES activity is regulated during the Streptomyces life cycle: activity increased as cells progressed from exponential growth to stationary phase in liquid culture, or from mycelial growth to sporulation on solid media. While mutations that interfere with S. coelicolor development late in its life cycle did not prevent this developmentally associated increase in RNase ES activity, the increase was blocked by a mutation (bldA) that interferes early with both morphological and physiological differentiation.

show abstract

mRNA degradation in procaryotes

Cited by 91 publications

References 1 publication

Determination of the Catalytic Parameters of the N-terminal Half of Escherichia coli Ribonuclease E and the Identification of Critical Functional Groups in RNA Substrates

Determination of the Catalytic Parameters of the N-terminal Half of Escherichia coli Ribonuclease E and the Identification of Critical Functional Groups in RNA Substrates

RNase E: still a wonderfully mysterious enzyme

A developmentally regulated Streptomyces endoribonuclease resembles ribonuclease E of Escherichia coli

Contact Info

Product

Resources

About