{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T14:36:28Z","timestamp":1781102188404,"version":"3.54.1"},"reference-count":41,"publisher":"National Academy of Sciences","issue":"8","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2001,4,10]]},"abstract":"<jats:p>Intracellular protein degradation, which must be tightly controlled\n to protect normal proteins, is carried out by ATP-dependent proteases.\n These multicomponent enzymes have chaperone-like ATPases that\n recognize and unfold protein substrates and deliver them to the\n proteinase components for digestion. In ClpAP, hexameric rings of the\n ClpA ATPase stack axially on either face of the ClpP proteinase, which\n consists of two apposed heptameric rings. We have used cryoelectron\n microscopy to characterize interactions of ClpAP with the model\n substrate, bacteriophage P1 protein, RepA. In complexes stabilized by\n ATP\u03b3S, which bind but do not process substrate, RepA dimers are seen\n at near-axial sites on the distal surface of ClpA. On ATP addition,\n RepA is translocated through \u2248150 \u212b into the digestion chamber\n inside ClpP. Little change is observed in ClpAP, implying that\n translocation proceeds without major reorganization of the ClpA\n hexamer. When translocation is observed in complexes containing a ClpP\n mutant whose digestion chamber is already occupied by unprocessed\n propeptides, a small increase in density is observed within ClpP, and\n RepA-associated density is also seen at other axial sites. These sites\n appear to represent intermediate points on the translocation pathway,\n at which segments of unfolded RepA subunits transiently accumulate en\n route to the digestion chamber.<\/jats:p>","DOI":"10.1073\/pnas.081543698","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:44:19Z","timestamp":1027680259000},"page":"4328-4333","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":118,"title":["Translocation pathway of protein substrates in ClpAP protease"],"prefix":"10.1073","volume":"98","author":[{"given":"Takashi","family":"Ishikawa","sequence":"first","affiliation":[{"name":"Laboratory of Structural Biology, National Institute\r of Arthritis, Musculoskeletal and Skin Diseases, and Laboratories of\r Cell Biology and Molecular Biology,\r National Cancer Institute, National Institutes of Health, Bethesda, MD\r 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fabienne","family":"Beuron","sequence":"additional","affiliation":[{"name":"Laboratory of Structural Biology, National Institute\r of Arthritis, Musculoskeletal and Skin Diseases, and Laboratories of\r Cell Biology and Molecular Biology,\r National Cancer Institute, National Institutes of Health, Bethesda, MD\r 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martin","family":"Kessel","sequence":"additional","affiliation":[{"name":"Laboratory of Structural Biology, National Institute\r of Arthritis, Musculoskeletal and Skin Diseases, and Laboratories of\r Cell Biology and Molecular Biology,\r National Cancer Institute, National Institutes of Health, Bethesda, MD\r 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sue","family":"Wickner","sequence":"additional","affiliation":[{"name":"Laboratory of Structural Biology, National Institute\r of Arthritis, Musculoskeletal and Skin Diseases, and Laboratories of\r Cell Biology and Molecular Biology,\r National Cancer Institute, National Institutes of Health, Bethesda, MD\r 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael R.","family":"Maurizi","sequence":"additional","affiliation":[{"name":"Laboratory of Structural Biology, National Institute\r of Arthritis, Musculoskeletal and Skin Diseases, and Laboratories of\r Cell Biology and Molecular Biology,\r National Cancer Institute, National Institutes of Health, Bethesda, MD\r 20892"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alasdair C.","family":"Steven","sequence":"additional","affiliation":[{"name":"Laboratory of Structural Biology, National Institute\r of Arthritis, Musculoskeletal and Skin Diseases, and Laboratories of\r Cell Biology and Molecular Biology,\r National Cancer Institute, National Institutes of Health, Bethesda, MD\r 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