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The SF2 helicase RecG is a key enzyme in the processing of postreplication gaps or regressed forks in Escherichia coli. A deletion of the recG gene renders cells highly sensitive to a range of DNA damaging agents. Here, we demonstrate that RecG function is at least partially complemented by another SF2 helicase, RadD. A \u0394recG\u0394radD double mutant exhibits an almost complete growth defect, even in the absence of stress. Suppressors appear quickly, primarily mutations that compromise priA helicase function or recA promoter mutations that reduce recA expression. Deletions of uup (encoding the UvrA-like ABC system Uup), recO, or recF also suppress the \u0394recG\u0394radD growth phenotype. RadD and RecG appear to avoid toxic situations in DNA metabolism, either resolving or preventing the appearance of DNA repair intermediates produced by RecA or RecA-independent template switching at stalled forks or postreplication gaps. Barriers to replisome progress that require intervention by RadD or RecG occur in virtually every replication cycle. The results highlight the importance of the RadD protein for general chromosome maintenance and repair. They also implicate Uup as a new modulator of RecG function.<\/jats:p>","DOI":"10.1093\/nar\/gkaa579","type":"journal-article","created":{"date-parts":[[2020,6,26]],"date-time":"2020-06-26T20:28:31Z","timestamp":1593203311000},"page":"8445-8460","source":"Crossref","is-referenced-by-count":31,"title":["Resolving Toxic DNA repair intermediates in every E.\u00a0coli replication cycle: critical roles for RecG, Uup and RadD"],"prefix":"10.1093","volume":"48","author":[{"given":"Zachary J","family":"Romero","sequence":"first","affiliation":[{"name":"Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefanie H","family":"Chen","sequence":"additional","affiliation":[{"name":"Biotechnology Program, North Carolina State University, Raleigh, NC 27695, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas","family":"Armstrong","sequence":"additional","affiliation":[{"name":"Molecular Horizons Institute and School of Chemistry, University of Wollongong, Wollongong, Australia"},{"name":"Illawarra Health and Medical Research Institute, Wollongong, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elizabeth A","family":"Wood","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antoine","family":"van\u00a0Oijen","sequence":"additional","affiliation":[{"name":"Molecular Horizons Institute and School of Chemistry, University of Wollongong, Wollongong, Australia"},{"name":"Illawarra Health and Medical Research Institute, Wollongong, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3544-0976","authenticated-orcid":false,"given":"Andrew","family":"Robinson","sequence":"additional","affiliation":[{"name":"Molecular Horizons Institute and School of Chemistry, University of Wollongong, Wollongong, Australia"},{"name":"Illawarra Health and Medical Research Institute, Wollongong, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3606-5722","authenticated-orcid":false,"given":"Michael M","family":"Cox","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2020,7,9]]},"reference":[{"key":"2020090320025397300_B1","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/j.resmic.2004.01.018","article-title":"When replication travels on damaged templates: bumps and blocks in the road","volume":"155","author":"Courcelle","year":"2004","journal-title":"Res. 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