Author

S. A. Darst

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 9 Biochemistry· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 11 Assay:cryo-EM· 6 Research Focus:chromatin & epigenetic regulation· 5 Assay:structural biology· 5 Organism:virus· 5 Research Focus:protein structure prediction· 3 Research Focus:drug response / drug discovery· 2 Organism:E. coli· 2

Frequent Co-Authors

E. A. Campbell· 9 shared J. Chen· 9 shared E. Llewellyn· 5 shared E. T. Eng· 5 shared P. D. B. Olinares· 5 shared B. Malone· 4 shared R. Landick· 4 shared B. T. Chait· 3 shared

Activity by Year

2018-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 35 mutual co-author links

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9 shared papersBiophysics

E. A. Campbell

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Author profile →

12 papers

Recent·Most cited

Structural and functional insights into the enzymatic plasticity of the SARS-CoV-2 NiRAN Domain

G. I. Small, O. Federova, P. D. B. Olinares, J. Chandanani, A. Banerjee, Y. J. Choi, H. Molina, B. Chait, S. A. Darst, E. A. Campbell

This study determines cryo-EM structures of SARS-CoV-2 NiRAN domain catalytic intermediates, revealing structural mechanisms for NMPylation and deRNAylation/capping, and explaining substrate preference for capping.

bioRxiv · Sep 25, 2023Biophysics

Discovery, Characterization, and Bioactivity of the Achromonodins: Lasso Peptides Encoded by Achromobacter

D. V. Carson, Y. Zhang, L. So, W. L. Cheung-Lee, A. J. Cartagena, S. A. Darst, A. J. Link

The paper discovers and characterizes two lasso peptides from Achromobacter species, showing one inhibits RNA polymerase and has antimicrobial activity against Achromobacter pulmonis.

bioRxiv · Jun 21, 2023Biochemistry

An ensemble of interconverting conformations of the elemental paused transcription complex creates regulatory options

J. Y. Kang, T. V. Mishanina, Y. Bao, J. Chen, E. Llewellyn, J. Liu, S. A. Darst, R. Landick

This study defines an interconverting ensemble of ePEC states using cryo-EM and biochemical analysis, showing that ePECs occupy pre- or half-translocated states without always swiveling.

bioRxiv · Sep 11, 2022Biochemistry

Structural basis for substrate selection by the SARS-CoV-2 replicase

B. F. Malone, J. K. Perry, P. D. B. Olinares, J. Chen, T. K. Appleby, J. Y. Feng, J. P. Bilello, H. Ng, J. Sotiris, M. Ebrahim, E. Y. D. Chua, J. H. Mendez, E. T. Eng, R. Landick, B. T. Chait, , S. A. Darst

This study uses cryo-EM to reveal how the SARS-CoV-2 RTC discriminates between natural NTPs and the antiviral remdesivir triphosphate, providing insights for antiviral design.

bioRxiv · May 20, 2022Biophysics

Ensemble cryo-electron microscopy reveals conformational states of the nsp13 helicase in the SARS-CoV-2 helicase replication-transcription complex

J. Chen, Q. Wang, B. Malone, E. Llewellyn, Y. Pechersky, K. Maruthi, E. T. Eng, J. K. Perry, E. A. Campbell, D. E. Shaw, S. A. Darst

This study uses cryo-EM and simulations to identify four conformational states of the nsp13 helicase in the SARS-CoV-2 RTC, revealing an allosteric mechanism for switching between RNA synthesis and backtracking.

bioRxiv · Nov 10, 2021 · PreprintBiophysics

Structural origins of Escherichia coli RNA polymerase open promoter complex stability

R. M. Saecker, J. Chen, C. E. Chiu, B. Malone, J. Sortiris, M. Ebrahim, L. Y. Yen, E. T. Eng, S. A. Darst

This study determines the structural basis of RNA polymerase open complex stability in E. coli by analyzing three promoters with different lifetimes using cryo-EM.

bioRxiv · Sep 8, 2021Biophysics

Structural basis for backtracking by the SARS-CoV-2 replication-transcription complex

B. Malone, J. Chen, Q. Wang, E. Llewellyn, Y. J. Choi, P. D. B. Olinares, X. Cao, C. Hernandez, E. T. Eng, B. T. Chait, D. E. Shaw, R. Landick, S. A. Darst, E. A. Campbell

This paper shows that SARS-CoV-2 RdRp undergoes backtracking, which may aid proofreading and antiviral resistance.

bioRxiv · Mar 13, 2021Biochemistry

Structural basis for helicase-polymerase coupling in the SARS-CoV-2 replication-transcription complex

J. Chen, B. Malone, E. Llewellyn, M. Grasso, P. M. M. Shelton, P. D. B. Olinares, K. Maruthi, E. T. Eng, H. Vatandaslar, B. Chait, T. Kapoor, S. A. Darst, E. A. Campbell

The paper presents cryo-EM structures of the SARS-CoV-2 holo-RdRp complex with nsp13 helicase, revealing interactions and a new therapeutic target.

Cell · Sep 1, 2020Peer-reviewedBiophysics

Structural basis for transcription complex disruption by the Mfd translocase

J. Y. Kang, E. Llewellyn, J. Chen, P. D. B. Olinares, J. Brewer, B. T. Chait, E. A. Campbell, S. A. Darst

The paper uses cryo-EM to visualize Mfd interacting with stalled RNA polymerase complexes, revealing its mechanism for initiating transcription-coupled repair.

bioRxiv · Aug 12, 2020Biophysics

E. coli TraR allosterically regulates transcription initiation by altering RNA polymerase conformation and dynamics

J. Chen, S. Gopalkrishnan, C. Chiu, A. Y. Chen, E. A. Campbell, R. L. Gourse, W. Ross, S. A. Darst

This study shows TraR regulates transcription by altering RNAP conformation and dynamics, affecting promoter DNA interactions and transcription outcomes.

bioRxiv · Sep 12, 2019Biophysics

Structural basis for transcription activation by Crl through tethering of σS and RNA polymerase

A. J. Cartagena, A. B. Banta, N. Sathyan, W. Ross, R. L. Gourse, E. A. Campbell, S. A. Darst

The paper determines the cryo-EM structure of Crl-σS-RNAP complex and shows Crl stabilizes σS-RNAP by tethering σS to RNAP βCT.

bioRxiv · Aug 6, 2019Biophysics

Fidaxomicin jams M. tuberculosis RNA polymerase motions needed for initiation via RbpA contacts

H. Boyaci, J. Chen, M. Lilic, M. Palka, R. A. Mooney, R. Landick, S. A. Darst, E. A. Campbell

This study determines the structure of M. tuberculosis RNA polymerase with fidaxomicin, revealing how it inhibits transcription by blocking essential motions.

bioRxiv · Jan 8, 2018Biophysics