The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Polynucleotide phosphorylase functions both as a 3′ → 5′ exonuclease and a poly(A) polymerase in Escherichia coli
Open accessAbstract
In vitro , polynucleotide phosphorylase of Escherichia coli can both synthesize RNA by using nucleotide diphosphates as precursors and exonucleolytically degrade RNA in the presence of inorganic phosphate. However, because of the high in vivo concentration of inorganic phosphate in exponentially growing cells, it has been assumed that the enzyme works exclusively as an exonuclease. Here we demonstrate that, contrary to this prediction, polynucleotide phosphorylase not only synthesizes long, highly heteropolymeric tails in vivo , but also accounts for all of the observed residual polyadenylylation in poly(A) polymerase I deficient strains. In addition, the enzyme is responsible for adding the C and U residues that are found in poly(A) tails in exponentially growing cultures of wild type E. coli .
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Cites
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The Many Pathways of RNA Degradation
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The RNA Degradosome of Escherichia coli: An mRNA-Degrading Machine Assembled on RNase E
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Background
Metadata
- Authors
- Mohanty, B. K., & Kushner, S. R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-10-17
- Volume
- 97
- Issue
- 22
- Pages
- 11966-11971
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1653560622
- Cited by
- 266
- References
- 19
- FWCI
- 2.70
- Type
- journal article
- Language
- en
- Open access
- green
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- Mohanty, B. K., & Kushner, S. R. (2000). Polynucleotide phosphorylase functions both as a 3′ → 5′ exonuclease and a poly(A) polymerase in Escherichia coli. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.220295997
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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