Transcription Termination Factor Rho: A Ring-Shaped RNA Helicase from Bacteria
Transcription Termination Factor Rho: A Ring-Shaped RNA Helicase from Bacteria
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DOI:
10.1039/9781849732215-00243
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发表时间:
2010-01-01
期刊:
影响因子:
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通讯作者:
Boudvillain, Marc
中科院分区:
文献类型:
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作者:
Rabhi, Makhlouf;Rahmouni, A. Rachid;Boudvillain, Marc
Many NTP-dependent protein machines form oligomeric structures resembling doughnouts. 1-3 Such ring-shaped machines include DNA translocases such as viral DNA packaging motors or chromosomal segregation enzymes as well as numerous DNA helicases involved in recombination and replication. 1, 6–8 In contrast, only a few NTPases working on RNA are known to form oligomeric rings. 9-12 These include viral helicases involved in the replication and/or packaging of (+)-strand RNA viruses, 13, 14 the large T antigen from simian virus 40 (a double-stranded DNA virus), 15 and the P4 packaging motor pro-teins from Cystoviridae phages (our unpublished observations and ref. 16; see also Chapter 9). The transcription termination factor Rho from Escherichia coli, the subject of this review, is also a ring-shaped, hexameric enzyme that displays ATP-dependent RNA and RNA-DNA helicase activities in vitro. 17, 18 Since its discovery in 1969, 19 Rho has become a classical transcription factor paradigm. The main, accepted biological function of Rho is the disruption of