The structural basis of DNA binding by the single-stranded DNA-binding protein from Sulfolobus solfataricus

Gamsjaeger, Roland, Kariawasam, Ruvini, Gimenez, Adrian X., Touma, Christine, McIlwain, Elysse, Bernardo, Ray E., Shepherd, Nicholas E., Ataide, Sandro F., Dong, Qihan, Richard, Derek J., White, Malcolm F. and Cubeddu, Liza (2015) The structural basis of DNA binding by the single-stranded DNA-binding protein from Sulfolobus solfataricus. Biochemical Journal, 465 337-346. doi:10.1042/BJ20141140


Author Gamsjaeger, Roland
Kariawasam, Ruvini
Gimenez, Adrian X.
Touma, Christine
McIlwain, Elysse
Bernardo, Ray E.
Shepherd, Nicholas E.
Ataide, Sandro F.
Dong, Qihan
Richard, Derek J.
White, Malcolm F.
Cubeddu, Liza
Title The structural basis of DNA binding by the single-stranded DNA-binding protein from Sulfolobus solfataricus
Formatted title
The structural basis of DNA binding by the single-stranded DNA-binding protein from Sulfolobus solfataricus
Journal name Biochemical Journal   Check publisher's open access policy
ISSN 1470-8728
0264-6021
Publication date 2015-01-15
Sub-type Article (original research)
DOI 10.1042/BJ20141140
Volume 465
Start page 337
End page 346
Total pages 10
Place of publication London, United Kingdom
Publisher Portland Press
Collection year 2016
Language eng
Formatted abstract
Canonical single-stranded DNA-binding proteins (SSBs) from the oligosaccharide/oligonucleotide-binding (OB) domain family are present in all known organisms and are critical for DNA replication, recombination and repair. The SSB from the hyperthermophilic crenarchaeote Sulfolobus solfataricus (SsoSSB) has a ‘simple’ domain organization consisting of a single DNA-binding OB fold coupled to a flexible C-terminal tail, in contrast with other SSBs in this family that incorporate up to four OB domains. Despite the large differences in the domain organization within the SSB family, the structure of the OB domain is remarkably similar all cellular life forms. However, there are significant differences in the molecular mechanism of ssDNA binding. We have determined the structure of the SsoSSB OB domain bound to ssDNA by NMR spectroscopy. We reveal that ssDNA recognition is modulated by base-stacking of three key aromatic residues, in contrast with the OB domains of human RPA and the recently discovered human homologue of SsoSSB, hSSB1. We also demonstrate that SsoSSB binds ssDNA with a footprint of five bases and with a defined binding polarity. These data elucidate the structural basis of DNA binding and shed light on the molecular mechanism by which these ‘simple’ SSBs interact with ssDNA.
Keyword Base-stacking
NMR
OB domain
Single-stranded DNA-binding protein
Sulfolobus solfataricus
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Non HERDC
Institute for Molecular Bioscience - Publications
 
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