Barbora Brezovska

Barbora Brezovska
  • Master of Science
  • Complex of Biomedical Institutes at Krč

About

7
Publications
773
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37
Citations
Introduction
In my work, I am focused on the key enzyme of bacterial transcription, RNA polymerase (RNAP). Firstly I am analysing various factors associating with RNAP. Specifically proteins HelD, CarD, RbpA and MoaB2, an interaction partners of RNAP from M. smegmatis. I am optimizing conditions of these transcription factors and defining their functions. Secondly I am studying several RNAP (E. coli, B. subtilis, M. smegmatis) and its interactions with modified nucleic acids (DNA and RNA).

Publications

Publications (7)
Article
Full-text available
In mycobacteria, σA is the primary sigma factor. This essential protein binds to RNA polymerase (RNAP) and mediates transcription initiation of housekeeping genes. Our knowledge about this factor in mycobacteria is limited. Here, we performed an unbiased search for interacting partners of Mycobacterium smegmatis σA. The search revealed a number of...
Article
Full-text available
Mycobacterial HelD is a transcription factor that recycles stalled RNAP by dissociating it from nucleic acids and, if present, from the antibiotic rifampicin. The rescued RNAP, however, must disengage from HelD to participate in subsequent rounds of transcription. The mechanism of release is unknown. We show that HelD from Mycobacterium smegmatis f...
Preprint
Full-text available
Chemical modifications of RNA affect essential properties of transcripts, such as their translation, localization and stability. 5-end RNA capping with the ubiquitous redox cofactor nicotinamide adenine dinucleotide (NAD+) has been discovered in organisms ranging from bacteria to mammals. However, the hypothesis that NAD+ capping might be universal...
Article
Full-text available
RNA synthesis is central to life, and RNA polymerase (RNAP) depends on accessory factors for recovery from stalled states and adaptation to environmental changes. Here, we investigated the mechanism by which a helicase-like factor HelD recycles RNAP. We report a cryo-EM structure of a complex between the Mycobacterium smegmatis RNAP and HelD. The c...
Preprint
Full-text available
RNA synthesis is central to life, and RNA polymerase depends on accessory factors for recovery from stalled states and adaption to environmental changes. Here we investigated the mechanism by which a helicase-like factor HelD recycles RNA polymerase. We report a cryo-EM structure of an unprecedented complex between the Mycobacterium smegmatis RNA p...

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