Hexameric Viral RNA Helicases
Hexameric Viral RNA Helicases
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DOI:
10.1039/9781849732215-00213
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发表时间:
2010-01-01
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影响因子:
--
通讯作者:
Tuma, Roman
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文献类型:
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作者:
Tuma, Roman
Hexameric helicases are widespread in DNA replication (eg, DnaB, the main replicative helicase in E. coli). Hexameric RNA helicases fulfill various functions ranging from transcription termination to virus replication and assembly. In contrast to the ubiquitous SF2 helicases there are only a few characterised hexameric helicases that unwind or translocate RNA. Most hexameric helicases are composed of identical subunits arranged into a ring around the central channel. Six identical ATP binding sites are located at subunit interfaces at the perimeter of the ring and encompass residues from neighbouring subunits. The central channel hosts nucleic-acid-binding sites, which are essential for helicase activity. While details are still being debated, the mechanism of unwinding most likely involves translocation along a nucleic acid strand bound within the central channel while the complementary strand is excluded by the ring (Figure 9.1 (A)). 1 The topological enclosure of the translocated strand assures processivity in a fashion similar to replicative DNA clamps, such as PCNA. Indeed, structural comparisons suggest that processivity clamps evolved from hexameric molecular motors through the loss of the ability to bind and hydrolyse ATP. 2