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  Mechanisms of backtrack recovery by RNA polymerases I and II.

Lisica, A., Engel, C., Jahnel, M., Roldán, É., Galburt, E. A., Cramer, P., et al. (2016). Mechanisms of backtrack recovery by RNA polymerases I and II. Proceedings of the National Academy of Sciences of the United States of America, 113(11), 2946-2951. doi:10.1073/pnas.1517011113.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-D5A9-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-DFC1-1
Genre: Journal Article

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 Creators:
Lisica, A., Author
Engel, C.1, Author              
Jahnel, M., Author
Roldán, É., Author
Galburt, E. A., Author
Cramer, P.1, Author              
Grill, S. W., Author
Affiliations:
1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

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Free keywords: Pol I; Pol II; backtracking; optical tweezers; transcription
 Abstract: During DNA transcription, RNA polymerases often adopt inactive backtracked states. Recovery from backtracks can occur by 1D diffusion or cleavage of backtracked RNA, but how polymerases make this choice is unknown. Here, we use single-molecule optical tweezers experiments and stochastic theory to show that the choice of a backtrack recovery mechanism is determined by a kinetic competition between 1D diffusion and RNA cleavage. Notably, RNA polymerase I (Pol I) and Pol II recover from shallow backtracks by 1D diffusion, use RNA cleavage to recover from intermediary depths, and are unable to recover from extensive backtracks. Furthermore, Pol I and Pol II use distinct mechanisms to avoid nonrecoverable backtracking. Pol I is protected by its subunit A12.2, which decreases the rate of 1D diffusion and enables transcript cleavage up to 20 nt. In contrast, Pol II is fully protected through association with the cleavage stimulatory factor TFIIS, which enables rapid recovery from any depth by RNA cleavage. Taken together, we identify distinct backtrack recovery strategies of Pol I and Pol II, shedding light on the evolution of cellular functions of these key enzymes.

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Language(s): eng - English
 Dates: 2016-03-15
 Publication Status: Published online
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1073/pnas.1517011113
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Title: Proceedings of the National Academy of Sciences of the United States of America
Source Genre: Journal
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Pages: - Volume / Issue: 113 (11) Sequence Number: - Start / End Page: 2946 - 2951 Identifier: -