Degradation of mRNA in bacteria: emergence of ubiquitous features

Régnier, Philippe; Arraiano, Cecília M.

doi:10.1002/(sici)1521-1878(200003)22:3<235::aid-bies5>3.0.co;2-2

Cited by 163 publications

(20 citation statements)

References 85 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Escherichia coli double mutants lacking these genes were still viable and any defects in protein folding were observed during its growth [34]. In the present study, the abundance of polynucleotide phopshorylase/ polyadenylase protein (PNPase, spot 717; p-value = 0.002) decreased but only at 48 h compared to 8 h. This protein is related to the mRNA degradation system in bacteria [35]. Yehudai-Resheff et al [36] assumed that a high concentration of phosphorus in bacteria enhanced PNPase degradation activity.…”

Section: Stress Responsementioning

confidence: 48%

Proteomic Response of Pseudomonas putida KT2440 to Dual Carbon-Phosphorus Limitation during mcl-PHAs Synthesis

Możejko-Ciesielska

Serafim

2019

Biomolecules

View full text Add to dashboard Cite

Pseudomonas putida KT2440, one of the best characterized pseudomonads, is a metabolically versatile producer of medium-chain-length polyhydroxyalkanoates (mcl-PHAs) that serves as a model bacterium for molecular studies. The synthesis of mcl-PHAs is of great interest due to their commercial potential. Carbon and phosphorus are the essential nutrients for growth and their limitation can trigger mcl-PHAs’ production in microorganisms. However, the specific molecular mechanisms that drive this synthesis in Pseudomonas species under unfavorable growth conditions remain poorly understood. Therefore, the proteomic responses of Pseudomonas putida KT2440 to the limited carbon and phosphorus levels in the different growth phases during mcl-PHAs synthesis were investigated. The data indicated that biopolymers’ production was associated with the cell growth of P. putida KT2440 under carbon- and phosphorus-limiting conditions. The protein expression pattern changed during mcl-PHAs synthesis and accumulation, and during the different physiological states of the microorganism. The data suggested that the majority of metabolic activities ceased under carbon and phosphorus limitation. The abundance of polyhydroxyalkanoate granule-associated protein (PhaF) involved in PHA synthesis increased significantly at 24 and 48 h of the cultivations. The activation of proteins belonging to the phosphate regulon was also detected. Moreover, these results indicated changes in the protein profiles related to amino acids metabolism, replication, transcription, translation, stress response mechanisms, transport or signal transduction. The presented data allowed the investigation of time-course proteome alterations in response to carbon and phosphorus limitation, and PHAs synthesis. This study provided information about proteins that can be potential targets in improving the efficiency of mcl-PHAs synthesis.

show abstract

Section: Stress Responsementioning

confidence: 48%

Proteomic Response of Pseudomonas putida KT2440 to Dual Carbon-Phosphorus Limitation during mcl-PHAs Synthesis

Możejko-Ciesielska

Serafim

2019

Biomolecules

View full text Add to dashboard Cite

show abstract

“…Regulation of mRNA stability provides a potent mechanism for governing gene expression. In bacteria, mRNA decay not only expedites adaptation of patterns of protein synthesis to changing environmental conditions, but also enables ribonucleotide salvage and differential expression of genes encoded by polycistronic mRNAs (Grunberg‐Manago, 1999; Rauhut and Klug, 1999; Régnier and Arraiano, 2000). In Escherichia coli , the degradation of many, if not most, mRNAs is initiated by an endonucleolytic cleavage catalysed by RNase E (Cohen and McDowall, 1997; Coburn and Mackie, 1999; Carpousis et al ., 1999; Steege, 2000).…”

Section: Introductionmentioning

confidence: 99%

Ectopic RNase E sites promote bypass of 5′‐end‐dependent mRNA decay in Escherichia coli

Baker

Mackie

2002

Molecular Microbiology

105

View full text Add to dashboard Cite

SummaryIn Escherichia coli , 5 ¢ ¢ ¢ ¢ -terminal stem-loops form major impediments to mRNA decay, yet conditions that determine their effectiveness or the use of alternative decay pathway(s) are unclear. A synthetic 5 ¢ ¢ ¢ ¢ -terminal hairpin stabilizes the rpsT mRNA sixfold. This stabilization is dependent on efficient translational initiation and ribosome transit through at least two-thirds of the coding sequence past a major RNase E cleavage site in the rpsT mRNA. Insertion of a 12-15 residue 'ectopic' RNase E cleavage site from either the rne leader or 9S pre-rRNA into the 5 ¢ ¢ ¢ ¢ -non-coding region of the rpsT mRNA significantly reduces the stabilizing effect of the terminal stem-loop, dependent on RNase E. A similar insertion into the rpsT coding sequence is partially destabilizing. These findings demonstrate that RNase E can bypass an interaction with the 5 ¢ ¢ ¢ ¢ -terminus, and exploit an alternative 'internal entry' pathway. We propose a model for degradation of the rpsT mRNA, which explains the hierarchy of protection afforded by different 5 ¢ ¢ ¢ ¢ -termini, the use of internal entry for bypass of barriers to decay, 'ectopic sites' and the role of translating ribosomes.

show abstract

“…In addition to the above processes of genetic expression, helicases also function as components of more esoteric macromolecular machines. For example, the RNA degradosome (for reviews see Carpousis et al 1999 ;Rauhut & Klug, 1999 ;Regnier & Arraiano, 2000) and the ribosomal translation machinery of the cell (see Lorsch & Herschlag, 1998a, b), both incorporate one or more helicases as integral components. In another very different system, the packaging of dsNA into viral capsids involves helicases that are anchored within the capsid and form a central part of the ' head-filling ' apparatus (Catalano, 2000;King et al 2001).…”

Section: Helicases As Components Of Macromolecular Machinesmentioning

confidence: 99%

Helicase mechanisms and the coupling of helicases within macromolecular machines Part II: Integration of helicases into cellular processes

Delagoutte

Hippel

2003

Quart. Rev. Biophys.

139

110

View full text Add to dashboard Cite

In Part I of this review [Delagoutte & von Hippel, Quarterly Reviews of Biophysics (2002) 35, 431-478] we summarized what is known about the properties, mechanisms, and structures of the various helicases that catalyze the unwinding of double-stranded nucleic acids. Here, in Part II, we consider these helicases as tightly integrated (or coupled) components of the various macromolecular machines within which they operate. The biological processes that are considered explicitly include DNA replication, recombination, and nucleotide excision repair, as well as RNA transcription and splicing. We discuss the activities of the constituent helicases (and their protein partners) in the assembly (or loading) of the relevant complex onto (and into) the specific nucleic acid sites at which the actions of the helicase-containing complexes are to be initiated, the mechanisms by which the helicases (and the complexes) translocate along the nucleic acids in discharging their functions, and the reactions that are used to terminate the translocation of the helicase-containing complexes at specific sites within the nucleic acid 'substrate'. We emerge with several specific descriptions of how helicases function within the above processes of genetic expression which, we hope, can serve as paradigms for considering how helicases may also be coupled and function within other macromolecular machines.

show abstract

Degradation of mRNA in bacteria: emergence of ubiquitous features

Cited by 163 publications

References 85 publications

Proteomic Response of Pseudomonas putida KT2440 to Dual Carbon-Phosphorus Limitation during mcl-PHAs Synthesis

Proteomic Response of Pseudomonas putida KT2440 to Dual Carbon-Phosphorus Limitation during mcl-PHAs Synthesis

Ectopic RNase E sites promote bypass of 5′‐end‐dependent mRNA decay in Escherichia coli

Helicase mechanisms and the coupling of helicases within macromolecular machines Part II: Integration of helicases into cellular processes

Contact Info

Product

Resources

About