{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,9]],"date-time":"2026-06-09T23:17:16Z","timestamp":1781047036958,"version":"3.54.1"},"reference-count":40,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2020,6,16]],"date-time":"2020-06-16T00:00:00Z","timestamp":1592265600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2021,2]]},"abstract":"<jats:p><jats:italic>Helicobacter\u00a0pylori<\/jats:italic> is the most infectious human pathogen that causes gastritis, peptic ulcers and stomach cancer. <jats:italic>H.\u00a0pylori<\/jats:italic> DNA polymerase I (HpPol I) is found to be essential for the viability of <jats:italic>H.\u00a0pylori<\/jats:italic>, but its intrinsic property and attribution to the <jats:italic>H.\u00a0pylori<\/jats:italic> DNA replication remain unclear. HpPol I contains a 5\u2032\u21923\u2032 exonuclease (5\u2032\u2010Exo) and DNA polymerase (Pol) domain, respectively, but lacks a 3\u2032\u21925\u2032 exonuclease, or error proofreading activity. In this study, we characterized the 5\u2032\u2010Exo and Pol functions of HpPol I and found that HpPol I is a multifunctional protein displaying DNA nick translation, strand\u2010displacement synthesis, RNase H\u2010like, structure\u2010specific endonuclease and exonuclease activities. In the <jats:italic>in\u00a0vitro<\/jats:italic> DNA replication assay, we further demonstrated that the 5\u2032\u2010Exo and Pol domains of HpPol I can cooperate to fill in the DNA gap, remove the unwanted RNA primer from a RNA\/DNA hybrid and create a ligatable nick for the DNA ligase A of <jats:italic>H.\u00a0pylori<\/jats:italic> to restore the normal duplex DNA. Altogether, our study suggests that the two catalytic domains of HpPol I may synergistically play an important role in the maturation of Okazaki fragments during the lagging\u2010strand DNA synthesis in <jats:italic>H.\u00a0pylori<\/jats:italic>. Like the functions of DNA polymerase I in <jats:italic>Escherichia\u00a0coli<\/jats:italic>, HpPol I may involve in both DNA replication and repair in <jats:italic>H.\u00a0pylori.<\/jats:italic><\/jats:p>","DOI":"10.1111\/febs.15434","type":"journal-article","created":{"date-parts":[[2020,6,2]],"date-time":"2020-06-02T10:09:21Z","timestamp":1591092561000},"page":"884-901","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["A multifunctional DNA polymerase I involves in the maturation of Okazaki fragments during the lagging\u2010strand DNA synthesis in <i>Helicobacter\u00a0pylori<\/i>"],"prefix":"10.1111","volume":"288","author":[{"given":"Yi\u2010Wen","family":"Cheng","sequence":"first","affiliation":[{"name":"Department of Medical Laboratory Science and Biotechnology College of Medicine National Cheng Kung University Tainan City 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