Supplemental Material can be found at:

http://www.jbc.org/content/suppl/2011/04/01/286.14.e99922.DCAuth
or_profile.html

Papers of the Week

Visualizing Stalled DNA Replication Repair
See referenced article, J. Biol. Chem. 2011, 286, 1207512085
Structure and Biochemical Activities of Escherichia coli MgsA

DOI 10.1074/jbc.P110.210187
e99922

Downloaded from www.jbc.org by guest, on April 3, 2011

In bacteria, DNA replication forks stall when they

encounter obstacles such as DNA lesions, template
strand breaks, and DNA-bound proteins. Stalled replication forks can occur as often as once per cell generation during normal cell growth and must be repaired
for the cell to function properly. The bacterial maintenance of genome stability protein A (MgsA) and its
related eukaryotic enzymes play important roles in
cellular responses to stalled DNA replication, most
probably by facilitating recovery of the replication
forks. Although sequencing has shown that MgsA enzymes are members of the clamp loader clade of AAA
(ATPases associated with a variety of cellular activities) proteins, there is little information about how
they function. In this Paper of the Week, Asher N. Page
The structure of E. coli MgsA. The crystalloand colleagues describe the x-ray crystal structure of graphic asymmetric unit is shown with one
protomer in ribbon form and the three remaining
E. coli MgsA, revealing that the enzyme is a te- protomers in surface form.
trameran interesting departure from the other pentameric AAA proteins that function in DNA metabolism. The researchers also show that
MgsA has biochemical properties similar to those of the eukaryotic orthologs and that the
enzyme binds the single-stranded DNA-binding protein (SSB) largely through its C-terminal
tail. This is an interesting investigation of a conserved genome stability protein whose function
remains enigmatic in prokaryotes and in eukaryotes.