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The mechanism of DNA replication primer synthesis by RNA polymerase

Nikolay Zenkin
Tatyana Naryshkina
Konstantin Severinov
Research02 Feb 2006
Nature

Volume: 439, P: 617-620
Translation selectively destroys non-functional transcription complexes

Translation actively dislodges stalled transcription elongation complexes (ECs) from damaged DNA, which enables lesion repair and restoration of transcription activity, and coupled ribosomes discriminate between active ECs and stalled ECs, ensuring destruction of only the latter.

Jason Woodgate
Hamed Mosaei
Nikolay Zenkin
ResearchOpen Access07 Feb 2024
Nature

Volume: 626, P: 891-896
Single-peptide DNA-dependent RNA polymerase homologous to multi-subunit RNA polymerase

Although all known RNA polymerases have multiple subunits, unrelated single-subunit polymerases have also been described. Here, the authors describe a single-subunit RNA polymerase from the SPβ prophage ofBacillus subtilis, which shares homology to multi-subunit enzymes.

David Forrest
Katherine James
Nikolay Zenkin
ResearchOpen Access06 Jun 2017
Nature Communications

Volume: 8, P: 1-8
The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu

The Doc-Phd toxin-antitoxin system inhibits bacterial translation via an unknown mechanism. Functional and structural analyses now show that Doc, which has an active site like AMPylating Fic proteins, actually works as a kinase, phosphorylating EF-Tu to block translation.

Daniel Castro-Roa
Abel Garcia-Pino
Nikolay Zenkin
Research20 Oct 2013
Nature Chemical Biology

Volume: 9, P: 811-817
The σ⁷⁰ subunit of RNA polymerase induces lacUV5 promoter-proximal pausing of transcription

Konstantin Brodolin
Nikolay Zenkin
Hermann Heumann
Research02 May 2004
Nature Structural & Molecular Biology

Volume: 11, P: 551-557