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  Phage P4 origin-binding domain structure reveals a mechanism for regulation of DNA-binding activity by homo- and heterodimerization of winged helix proteins

Yeo, H.-J., Ziegelin, G., Korolev, S., Calendar, R., Lanka, E., & Waksman, G. (2002). Phage P4 origin-binding domain structure reveals a mechanism for regulation of DNA-binding activity by homo- and heterodimerization of winged helix proteins. Molecular Microbiology, 43(4), 855-867.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-8C28-2 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-8C29-F
Genre: Journal Article
Alternative Title : Mol Microbiol

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 Creators:
Yeo, Hye-Jeong, Author
Ziegelin, Günter1, Author
Korolev, Sergey, Author
Calendar, Richard, Author
Lanka, Erich1, Author
Waksman, Gabriel, Author
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1Max Planck Society, ou_persistent13              

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 Abstract: The origin-binding domain of the gp protein of phage P4 (P4-OBD) mediates origin recognition and regulation of gp activity by the protein Cnr. We have determined the crystal structure of P4-OBD at 2.95 Å resolution. The structure of P4-OBD is that of a dimer with pseudo twofold symmetry. Each subunit has a winged helix topology with a unique structure among initiator proteins. The only structural homologue of the P4-OBD subunit is the DNA-binding domain of the eukaryotic transcriptional activator Rfx1. Based on this structural alignment, a model for origin recognition by the P4-OBD dimer is suggested. P4-OBD mutations that interfere with Cnr binding locate to the dimer interface, indicating that Cnr acts by disrupting the gp dimer. P4-OBD dimerization is mediated by helices 1 and 3 in both subunits, a mode of winged helix protein dimerization that is reminiscent of that of the eukaryotic transcription factors E2F and DP. This, in turn, suggests that Cnr is also a winged helix protein, a possibility that is supported by previously unreported sequence homologies between Cnr and Rfx1 and homology modelling. Hence, in a mechanism that appears to be conserved from phage to man, the DNA-binding activity of winged helix proteins can be regulated by other winged helix proteins via the versatile use of the winged helix motif as a homo- or heterodimerization scaffold.

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Language(s): eng - English
 Dates: 2002-03-27
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 24569
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Title: Molecular Microbiology
  Alternative Title : Mol Microbiol
Source Genre: Journal
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Pages: - Volume / Issue: 43 (4) Sequence Number: - Start / End Page: 855 - 867 Identifier: -