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Figure 8 | BMC Molecular Biology

Figure 8

From: Length-dependent degradation of single-stranded 3' ends by the Werner syndrome protein (WRN): implications for spatial orientation and coordinated 3' to 5' movement of its ATPase/helicase and exonuclease domains

Figure 8

Coordinated movement of WRN ATPase/helicase and exonuclease. Models for the concerted 3' to 5' movement of the ATPase/helicase and exonuclease domains of WRN on single-stranded (top) and 3' overhang substrates (bottom). WRN is shown as a bipartite complex with distinct helicase and exonuclease domains. At left is the suggested binding mode of WRN on a short (35 nt) oligomer or short (10 nt) 3' overhang substrate in the absence of ATP. ATP hydrolysis allows movement of the helicase domain in a 3' to 5' direction along either single-stranded or duplex DNA, with movement of the tethered exonuclease domain and concomitant stepwise degradation of DNA (indicated by dNMPs) in the same direction. On the 3' overhang substrate, ATP hydrolysis by WRN putatively mediates either translocation along the duplex without unwinding (upper pathway) or localized unwinding of the duplex (lower pathway).

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BMC Molecular Biology

ISSN: 1471-2199

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