Journal article
A distinctive single‐stranded DNA‐binding protein from the Archaeon Sulfolobus solfataricus
Molecular microbiology, Vol.43(6), pp.1505-1515
03/2002
Handle:
https://hdl.handle.net/2376/104867
PMID: 11971263
Abstract
Summary
Single‐stranded DNA binding proteins (SSBs) have been identified in all three domains of life. Here, we report the identification of a novel crenarchaeal SSB protein that is distinctly different from its euryar‐chaeal counterparts. Rather than comprising four DNA‐binding domains and a zinc‐finger motif within a single polypeptide of 645 amino acids, as for Methanococcus jannaschii, the Sulfolobus solfataricus
SSB protein (SsoSSB) has a single DNA‐binding domain in a polypeptide of just 148
amino acids with a eubacterial‐like acidic C‐terminus. SsoSSB protein was purified
to homogeneity and found to form tetramers in solution, suggesting a quaternary structure
analogous to that of E. coli SSB protein, despite possessing DNA‐binding domains
more similar to those of eukaryotic Replication Protein A (RPA). We demonstrate distributive
binding of SsoSSB to ssDNA at high temperature with an apparent site size of approximately
five nucleotides (nt) per monomer. Additionally, the protein is functional both in
vitro and in vivo, stimulating RecA protein‐mediated DNA strand‐exchange
and rescuing the ssb‐1 lethal mutation of E. coli respectively. We dis‐cuss possible evolutionary relationships amongst the various members of the SSB/RPA family.
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Details
- Title
- A distinctive single‐stranded DNA‐binding protein from the Archaeon Sulfolobus solfataricus
- Creators
- Cynthia A HaseltineStephen C Kowalczykowski
- Publication Details
- Molecular microbiology, Vol.43(6), pp.1505-1515
- Academic Unit
- Molecular Biosciences, School of
- Publisher
- Blackwell Science Ltd; Oxford, UK
- Number of pages
- 11
- Identifiers
- 99900546679501842
- Language
- English
- Resource Type
- Journal article