Document Type
Article
Language
eng
Format of Original
18 p.
Publication Date
11-2013
Publisher
Elsevier
Source Publication
Journal of Molecular Biology
Source ISSN
0022-2836
Original Item ID
DOI: 10.1016/j.jmb.2013.08.021
Abstract
Escherichia coli single-stranded DNA binding protein (SSB) plays essential roles in DNA replication, recombination and repair. SSB functions as a homotetramer with each subunit possessing a DNA binding domain (OB-fold) and an intrinsically disordered C-terminus, of which the last nine amino acids provide the site for interaction with at least a dozen other proteins that function in DNA metabolism. To examine how many C-termini are needed for SSB function, we engineered covalently linked forms of SSB that possess only one or two C-termini within a four-OB-fold “tetramer”. Whereas E. coli expressing SSB with only two tails can survive, expression of a single-tailed SSB is dominant lethal. E. coli expressing only the two-tailed SSB recovers faster from exposure to DNA damaging agents but accumulates more mutations. A single-tailed SSB shows defects in coupled leading and lagging strand DNA replication and does not support replication restart in vitro. These deficiencies in vitro provide a plausible explanation for the lethality observed in vivo. These results indicate that a single SSB tetramer must interact simultaneously with multiple protein partners during some essential roles in genome maintenance.
Recommended Citation
Antony, Edwin; Weiland, Elizabeth; Yuan, Quan; Manhart, Carol M.; Nguyen, Binh; Kozlov, Alexander G.; McHenry, Charles S.; and Lohman, Timothy M., "Multiple C-Terminal Tails within a Single E. coli SSB Homotetramer Coordinate DNA Replication and Repair" (2013). Biological Sciences Faculty Research and Publications. 420.
https://epublications.marquette.edu/bio_fac/420
Comments
Accepted version. Journal of Molecular Biology, Vol. 425, No. 23 (November 2013): 4802-4819. DOI.
NOTICE: this is the author’s version of a work that was accepted for publication in Journal of Molecular Biology. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Journal of Molecular Biology, VOL 425, ISSUE 23, November 2013, DOI.
Edwin Antony was affiliated with Washington University at the time of publication.