{
  "id": 2182329,
  "title": "Mutation of charged inner pore residues reduce E. coli β clamp residency and increase sliding rates on DNA",
  "url": "https://urgent.news/2026/08/20/mutation-of-charged-inner-pore-residues-reduce-e-coli-clamp-residency",
  "topic": "science",
  "section": "Science",
  "published": "2026-08-20T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.08.18.745641v1?rss=1"
  },
  "original_language": "en",
  "account": null,
  "summary": "Sliding clamp proteins play central roles in DNA metabolism, including replication and repair. The ring-shaped E. coli beta clamp accommodates double-stranded DNA and serves as a platform for proteins involved in multiple DNA transactions. The inner pore of the beta clamp harbors a series of positively charged and polar residues that can bind to the negatively charged backbone of the DNA. These…",
  "key_points": [],
  "editors_take": null,
  "illustration": null,
  "coverage": {
    "outlets": 1,
    "also_reported_by": []
  },
  "ai_generated": true,
  "disclaimer": "Summaries, key points and the editor’s take are written by software from other outlets’ reporting and may contain errors — always check the linked original."
}