Open Access
Proceedings of the National Academy of Sciences of the United States of America, volume 110, issue 51, pages 20437-20442
Rewriting the rules for end joining via enzymatic splicing of DNA 3′-PO4 and 5′-OH ends
1
Molecular Biology Program, Sloan-Kettering Institute, New York, NY 10065
Publication type: Journal Article
Publication date: 2013-11-11
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 11.1
ISSN: 00278424, 10916490
PubMed ID:
24218597
Multidisciplinary
Abstract
Significance The ability to repair breaks in the DNA phosphodiester backbone is essential for genome integrity. When breakage results in 5′-PO4 and 3′-OH termini, the ends can be rejoined to each other, or to novel partner strands, by classic DNA ligases that covalently activate the 5′-PO4 end by linkage to AMP. However, when breakage leaves 5′-OH and 3′-PO4 termini, the ends are considered “dirty” because they cannot be sealed by classic ligases. This paper shows that the unconventional ligase RtcB can evade the DNA dirty end chemistry problem by splicing DNA 3′-PO4 ends to DNA 5′-OH ends. RtcB accomplishes this by attaching a GMP nucleotide to the DNA 3′-PO4 end to activate it for nucleophilic attack by the 5′-OH. There are many biological contexts in which DNA damage generates “dirty” breaks with 3′-PO4 (or cyclic-PO4) and 5′-OH ends that cannot be sealed by DNA ligases. Here we show that the Escherichia coli RNA ligase RtcB can splice these dirty DNA ends via a unique chemical mechanism. RtcB transfers GMP from a covalent RtcB–GMP intermediate to a DNA 3′-PO4 to form a “capped” 3′ end structure, DNA3′pp5′G. When a suitable DNA 5′-OH end is available, RtcB catalyzes attack of the 5′-OH on DNA3′pp5′G to form a 3′–5′ phosphodiester splice junction. Our findings unveil an enzymatic capacity for DNA 3′ capping and the sealing of DNA breaks with 3′-PO4 and 5′-OH termini, with implications for DNA repair and DNA rearrangements.
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Das U. et al. Rewriting the rules for end joining via enzymatic splicing of DNA 3′-PO4 and 5′-OH ends // Proceedings of the National Academy of Sciences of the United States of America. 2013. Vol. 110. No. 51. pp. 20437-20442.
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Das U., Chakravarty A. K., Remus B. S., Shuman S. Rewriting the rules for end joining via enzymatic splicing of DNA 3′-PO4 and 5′-OH ends // Proceedings of the National Academy of Sciences of the United States of America. 2013. Vol. 110. No. 51. pp. 20437-20442.
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TY - JOUR
DO - 10.1073/pnas.1314289110
UR - https://doi.org/10.1073%2Fpnas.1314289110
TI - Rewriting the rules for end joining via enzymatic splicing of DNA 3′-PO4 and 5′-OH ends
T2 - Proceedings of the National Academy of Sciences of the United States of America
AU - Das, Ushati
AU - Chakravarty, Anupam K
AU - Remus, Barbara S
AU - Shuman, Stewart
PY - 2013
DA - 2013/11/11 00:00:00
PB - Proceedings of the National Academy of Sciences (PNAS)
SP - 20437-20442
IS - 51
VL - 110
PMID - 24218597
SN - 0027-8424
SN - 1091-6490
ER -
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@article{2013_Das,
author = {Ushati Das and Anupam K Chakravarty and Barbara S Remus and Stewart Shuman},
title = {Rewriting the rules for end joining via enzymatic splicing of DNA 3′-PO4 and 5′-OH ends},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
year = {2013},
volume = {110},
publisher = {Proceedings of the National Academy of Sciences (PNAS)},
month = {nov},
url = {https://doi.org/10.1073%2Fpnas.1314289110},
number = {51},
pages = {20437--20442},
doi = {10.1073/pnas.1314289110}
}
Cite this
MLA
Copy
Das, Ushati, et al. “Rewriting the rules for end joining via enzymatic splicing of DNA 3′-PO4 and 5′-OH ends.” Proceedings of the National Academy of Sciences of the United States of America, vol. 110, no. 51, Nov. 2013, pp. 20437-20442. https://doi.org/10.1073%2Fpnas.1314289110.