Cited by 29RNA and protein synthesis mechanismsForce Microscopy Techniques and ApplicationsRNA Research and Splicing

The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.

Direct observation of processive exoribonuclease motion using optical tweezers

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Fazal, Furqan M., Koslover, Daniel J., Luisi, Ben F., Block, Steven M.·2015·Proceedings of the National Academy of Sciences

Abstract

Significance: Bacteria regulate the synthesis and degradation of RNA molecules to ensure timely and robust responses to an ever-changing environment. The transcript’s lifetime can be influenced profoundly by a secondary structure that can form in the RNA and that may inhibit or promote its digestion by RNases. The molecular mechanisms by which RNases interact with structured RNAs therefore are of great interest. In this study we used optical tweezers to investigate the mechanistic properties of two such enzymes from Escherichia coli , polynucleotide phosphorylase and RNase R. Our results offer new insights into the functional characteristics of these two enzymes, including the sequence-dependent behavior of RNase R and the presence of discrete steps of six or seven nucleotides taken by polynucleotide phosphorylase.

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Crossref · 10.1073/pnas.1514028112

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  • The degradation speed of an mRNA polymer chain was taken to be 88 nt / s.

    “with the speed taken to be 88 nt / s.”

    From Bringing the genetically minimal cell to life on a computer in 4D (2026) · cites this paper as [96]

    The Results report an average RNase R velocity of 88 ± 8 nt/s, supporting the speed used in the citing sentence. That measurement was made on a dsRNA construct held at 20 pN; the paper does not establish 88 nt/s as the degradation speed of an mRNA polymer chain generally. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

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Metadata

Authors
Fazal, F. M., Koslover, D. J., Luisi, B. F., & Block, S. M.
Affiliations
  • Stanford University (US)
  • University of Cambridge (GB)
Corresponding author
Block, Steven M.
Venue
Proceedings of the National Academy of Sciences
Published
2015-11-23
Volume
112
Issue
49
Pages
15101-15106
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2261670798
Cited by
29
References
47
Citations by year
2026: 2 · 2024: 1 · 2023: 4 · 2022: 4 · 2021: 1 · 2020: 3 · 2019: 3 · 2018: 6 · 2017: 3 · 2016: 2
FWCI
1.59
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • HHS | NIH | National Institute of General Medical Sciences (GM057035)
  • Wellcome Trust (none)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
Keywords
RNase R, polynucleotide phosphorylase, RNA degradation, inchworm mechanism, RNA-binding domain, KH domain, S1 domain, Escherichia coli, helicase
MeSH terms
DNA, Exoribonucleases, RNA, Optical Tweezers

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