Structural basis of ECF-σ-factor-dependent transcription initiation

Lin, Wei; Mandal, Sukhendu; Degen, David; Cho, Min Sung; Feng, Yu; Das, Kalyan; Ebright, Richard H.

doi:10.1038/s41467-019-08443-3

Structural basis of ECF-σ-factor-dependent transcription initiation

Journal Article · Tue Feb 12 00:00:00 EST 2019 · Nature Communications

DOI:https://doi.org/10.1038/s41467-019-08443-3· OSTI ID:1498332

Lin, Wei ^[1]; ^[1]; Degen, David ^[1]; Cho, Min Sung ^[1]; Feng, Yu ^[1]; ^[2]; ^[1]

Rutgers Univ., Piscataway, NJ (United States)
Katholieke Univ. Leuven (Belgium)

Extracytoplasmic (ECF) σ factors, the largest class of alternative σ factors, are related to primary σ factors, but have simpler structures, comprising only two of six conserved functional modules in primary σ factors: region 2 (σR2) and region 4 (σR4). Here, we report crystal structures of transcription initiation complexes containing Mycobacterium tuberculosis RNA polymerase (RNAP), M. tuberculosis ECF σ factor σL, and promoter DNA. The structures show that σR2 and σR4 of the ECF σ factor occupy the same sites on RNAP as in primary σ factors, show that the connector between σR2 and σR4 of the ECF σ factor–although shorter and unrelated in sequence–follows the same path through RNAP as in primary σ factors, and show that the ECF σ factor uses the same strategy to bind and unwind promoter DNA as primary σ factors. The results define protein-protein and protein-DNA interactions involved in ECF-σ-factor-dependent transcription initiation.

View Accepted Manuscript (DOE)

Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: National Institutes of Health (NIH)

OSTI ID:: 1498332

Journal Information:: Nature Communications, Journal Name: Nature Communications Journal Issue: 1 Vol. 10; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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