ArticleRNA (New York, N.Y.)2001
Chloroplast PNPase exists as a homo-multimer enzyme complex that is distinct from the Escherichia coli degradosome.
Article in RNA (New York, N.Y.), 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
28 citing papers in PubMed, 73 citations in OpenAlex.
- Dysregulated 3'-end processing of 18S pre-rRNA decreases mtPNPase efficiency in plant mitochondria.Nucleic acids research · 2026Article
- Phase-separated bacterial ribonucleoprotein bodies organize mRNA decay.Wiley interdisciplinary reviews. RNA · 2020Review
- Organellar and Secretory Ribonucleases: Major Players in Plant RNA Homeostasis.Plant physiology · 2020Article
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- Article
- RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region.RNA (New York, N.Y.) · 2014Article
- RHON1 is a novel ribonucleic acid-binding protein that supports RNase E function in the Arabidopsis chloroplast.Nucleic acids research · 2012Article
- The Zea mays glycine-rich RNA-binding protein MA16 is bound to a ribonucleotide(s) by a stable linkage.Journal of plant research · 2012Article
- Nucleoid-enriched proteomes in developing plastids and chloroplasts from maize leaves: a new conceptual framework for nucleoid functions.Plant physiology · 2012Article
- Antisense RNA protects mRNA from RNase E degradation by RNA-RNA duplex formation during phage infection.Nucleic acids research · 2011Article
- Interactions of linker proteins with the phycobiliproteins in the phycobilisome substructures of Gloeobacter violaceus.Photosynthesis research · 2010Article
- Megadalton complexes in the chloroplast stroma of Arabidopsis thaliana characterized by size exclusion chromatography, mass spectrometry, and hierarchical clustering.Molecular & cellular proteomics : MCP · 2010Article
- Abnormal physiological and molecular mutant phenotypes link chloroplast polynucleotide phosphorylase to the phosphorus deprivation response in Arabidopsis.Plant physiology · 2009Article
- Crystal structure of Escherichia coli PNPase: central channel residues are involved in processive RNA degradation.RNA (New York, N.Y.) · 2008Article
- The RNase E/G-type endoribonuclease of higher plants is located in the chloroplast and cleaves RNA similarly to the E. coli enzyme.RNA (New York, N.Y.) · 2008Article
- Analysis of the human polynucleotide phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterparts.RNA (New York, N.Y.) · 2008Article
- Dark-induced mRNA instability involves RNase E/G-type endoribonuclease cleavage at the AU-box and SD sequences in cyanobacteria.Molecular genetics and genomics : MGG · 2007Article
- Proteome dynamics during plastid differentiation in rice.Plant physiology · 2007Article
- Mammalian polynucleotide phosphorylase is an intermembrane space RNase that maintains mitochondrial homeostasis.Molecular and cellular biology · 2006Article
- RhlB helicase rather than enolase is the beta-subunit of the Escherichia coli polynucleotide phosphorylase (PNPase)-exoribonucleolytic complex.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Escherichia coli, the exoribonuclease polynucleotide phosphorylase (PNPase), the endoribonuclease RNase E, a DEAD-RNA helicase and the glycolytic enzyme enolase are associated with a high molecular weight complex, the degradosome. This complex has an important role in processing and degradation of RNA. Chloroplasts contain an exoribonuclease homologous to E. coli PNPase. Size exclusion chromatography revealed that chloroplast PNPase elutes as a 580-600 kDa complex, suggesting that it can form an enzyme complex similar to the E. coli degradosome. Biochemical and mass-spectrometric analysis showed, however, that PNPase is the only protein associated with the 580-600 kDa complex. Similarly, a purified recombinant chloroplast PNPase also eluted as a 580-600 kDa complex after gel filtration chromatography. These results suggest that chloroplast PNPase exists as a homo-multimer complex. No other chloroplast proteins were found to associate with chloroplast PNPase during affinity chromatography. Database analysis of proteins homologous to E. coli RNase E revealed that chloroplast and cyanobacterial proteins lack the C-terminal domain of the E. coli protein that is involved in assembly of the degradosome. Together, our results suggest that PNPase does not form a degradosome-like complex in the chloroplast. Thus, RNA processing and degradation in this organelle differ in several respects from those in E. coli.
Indexed as
Identifiers
11680851PMC1370190W2163085102What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.