A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase rho
Tekijät: Said Nelly, Hilal Tarek, Sunday Nicholas D, Khatri Ajay, Bürger Jörg, Mielke Thorsten, Belogurov Georgiy A, Loll Bernhard, Sen Ranjan, Artsimovitch Irina, Wahl Markus C
Kustantaja: AMER ASSOC ADVANCEMENT SCIENCE
Julkaisuvuosi: 2021
Journal: Science
Tietokannassa oleva lehden nimi: SCIENCE
Lehden akronyymi: SCIENCE
Artikkelin numero: eabd1673
Vuosikerta: 371
Numero: 6524
Sivujen määrä: 11
ISSN: 0036-8075
DOI: https://doi.org/10.1126/science.abd1673
Tiivistelmä
Factor-dependent transcription termination mechanisms are poorly understood. We determined a series of cryo-electron microscopy structures portraying the hexameric adenosine triphosphatase (ATPase) rho on a pathway to terminating NusA/NusG-modified elongation complexes. An open rho ring contacts NusA, NusG, and multiple regions of RNA polymerase, trapping and locally unwinding proximal upstream DNA. NusA wedges into the rho ring, initially sequestering RNA. Upon deflection of distal upstream DNA over the RNA polymerase zinc-binding domain, NusA rotates underneath one capping rho subunit, which subsequently captures RNA. After detachment of NusG and clamp opening, RNA polymerase loses its grip on the RNA:DNA hybrid and is inactivated. Our structural and functional analyses suggest that rho, and other termination factors across life, may use analogous strategies to allosterically trap transcription complexes in a moribund state.
Factor-dependent transcription termination mechanisms are poorly understood. We determined a series of cryo-electron microscopy structures portraying the hexameric adenosine triphosphatase (ATPase) rho on a pathway to terminating NusA/NusG-modified elongation complexes. An open rho ring contacts NusA, NusG, and multiple regions of RNA polymerase, trapping and locally unwinding proximal upstream DNA. NusA wedges into the rho ring, initially sequestering RNA. Upon deflection of distal upstream DNA over the RNA polymerase zinc-binding domain, NusA rotates underneath one capping rho subunit, which subsequently captures RNA. After detachment of NusG and clamp opening, RNA polymerase loses its grip on the RNA:DNA hybrid and is inactivated. Our structural and functional analyses suggest that rho, and other termination factors across life, may use analogous strategies to allosterically trap transcription complexes in a moribund state.
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