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While speed and fidelity arise from the polymerase\u2019s intrinsic catalytic and proofreading activities, processivity is typically attributed to the DNA sliding clamp that tethers the polymerase to DNA. However, additional mechanisms may also contribute. The T4 bacteriophage polymerase can exchange on-the-fly, a process likely contributing to its \u223c10-fold higher synthesis rate compared with human polymerases. Here, we reconstituted the T4 holoenzyme and polymerase exchange complexes using purified gp43 polymerase, gp45 sliding clamp, and a primer\u2013template DNA substrate. Cryo-electron microscopy (cryo-EM) analysis revealed either one or two polymerases bound to the clamp and DNA. In the one-polymerase complex, the DNA threads perpendicularly through the clamp, supporting processive synthesis. In contrast, the two-polymerase complex displays a markedly tilted DNA orientation, impeding sliding and representing exchange intermediates. Three distinct conformational states of the two-polymerase complex define a multistep exchange mechanism. To our knowledge, these findings provide the first molecular-level view of replicative polymerase exchange.<\/jats:p>","DOI":"10.1093\/nar\/gkaf1359","type":"journal-article","created":{"date-parts":[[2025,12,23]],"date-time":"2025-12-23T12:56:36Z","timestamp":1766494596000},"source":"Crossref","is-referenced-by-count":1,"title":["Structural insights into the exchange mechanism of a replicative DNA polymerase"],"prefix":"10.1093","volume":"53","author":[{"given":"Xiang","family":"Feng","sequence":"first","affiliation":[{"name":"Department of Structural Biology, Van Andel Institute , Grand Rapids, MI 49503 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michelle M","family":"Spiering","sequence":"additional","affiliation":[{"name":"Department of Chemistry, The Pennsylvania State University , University Park, PA 16802 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Almeida","family":"Ruda de Luna Santos","sequence":"additional","affiliation":[{"name":"Department of Structural Biology, Van Andel Institute , Grand Rapids, MI 49503 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephen J","family":"Benkovic","sequence":"additional","affiliation":[{"name":"Department of Chemistry, The Pennsylvania State University , University Park, PA 16802 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8085-8928","authenticated-orcid":false,"given":"Huilin","family":"Li","sequence":"additional","affiliation":[{"name":"Department of Structural Biology, Van Andel Institute , Grand Rapids, MI 49503 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2025,12,29]]},"reference":[{"key":"2025122905465214500_B1","doi-asserted-by":"publisher","first-page":"963","DOI":"10.1016\/0022-2836(76)90346-6","article-title":"DNA elongation rates and growing point distributions of wild-type phage T4 and a DNA-delay amber mutant","volume":"106","author":"McCarthy","year":"1976","journal-title":"J Mol Biol"},{"key":"2025122905465214500_B2","doi-asserted-by":"publisher","first-page":"363","DOI":"10.1016\/0092-8674(92)90505-7","article-title":"A question of time: replication origins of eukaryotic chromosomes","volume":"71","author":"Fangman","year":"1992","journal-title":"Cell"},{"key":"2025122905465214500_B3","volume-title":"Molecular Biology of the Cell","author":"Alberts","year":"2002"},{"key":"2025122905465214500_B4","first-page":"7160","article-title":"A constant rate of spontaneous mutation in DNA-based microbes","volume-title":"Proc Natl Acad Sci USA","author":"Drake","year":"1991"},{"key":"2025122905465214500_B5","doi-asserted-by":"publisher","first-page":"553","DOI":"10.1093\/genetics\/138.3.553","article-title":"Rates of spontaneous mutation in bacteriophage T4 are independent of host fidelity determinants","volume":"138","author":"Santos","year":"1994","journal-title":"Genetics"},{"key":"2025122905465214500_B6","doi-asserted-by":"publisher","first-page":"10881","DOI":"10.1073\/pnas.90.22.10881","article-title":"Rapid assembly of the bacteriophage T4 core replication complex on a linear primer\/template construct","volume":"90","author":"Kaboord","year":"1993","journal-title":"Proc Natl Acad Sci USA"},{"key":"2025122905465214500_B7","doi-asserted-by":"publisher","first-page":"1084","DOI":"10.1021\/bi9520747","article-title":"Dual role of the 44\/62 protein as a matchmaker protein and DNA polymerase chaperone during assembly of the bacteriophage T4 holoenzyme complex","volume":"35","author":"Kaboord","year":"1996","journal-title":"Biochemistry"},{"key":"2025122905465214500_B8","first-page":"3211","article-title":"Assembly of a functional replication complex without ATP hydrolysis: a direct interaction of bacteriophage T4 gp45 with T4 DNA polymerase","volume-title":"Proc Natl Acad Sci USA","author":"Reddy","year":"1993"},{"key":"2025122905465214500_B9","doi-asserted-by":"publisher","first-page":"1830","DOI":"10.1016\/S0021-9258(18)52369-3","article-title":"Stimulation of the processivity of the DNA polymerase of bacteriophage T4 by the polymerase accessory proteins. 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