{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,6]],"date-time":"2026-03-06T00:22:29Z","timestamp":1772756549010,"version":"3.50.1"},"reference-count":40,"publisher":"Proceedings of the National Academy of Sciences","issue":"12","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1999,6,8]]},"abstract":"<jats:p>\n            Lon protease and members of the Clp family of molecular chaperones and protease regulatory subunits contain homologous regions with properties expected for substrate-binding domains. Fragments corresponding to these sequences are stably and independently folded for Lon, ClpA, and ClpY. The corresponding regions from ClpB and ClpX are unstable. All five fragments exhibit distinct patterns of binding to three proteins that are protease substrates\n            <jats:italic>in vivo<\/jats:italic>\n            : the heat shock transcription factor \u03c3\n            <jats:sup>32<\/jats:sup>\n            , the SOS mutagenesis protein UmuD, and Arc repressor bearing the SsrA degradation tag. Recognition of UmuD is mediated through peptide sequences within a 24-residue N-terminal region whereas recognition of both \u03c3\n            <jats:sup>32<\/jats:sup>\n            and SsrA-tagged Arc requires sequences at the C terminus. These results indicate that the Lon and Clp proteases use the same mechanism of substrate discrimination and suggest that these related ATP-dependent bacterial proteases scrutinize accessible or disordered regions of potential substrates for the presence of specific targeting sequences.\n          <\/jats:p>","DOI":"10.1073\/pnas.96.12.6678","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T14:39:15Z","timestamp":1027694355000},"page":"6678-6682","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":152,"title":["Lon and Clp family proteases and chaperones share homologous substrate-recognition domains"],"prefix":"10.1073","volume":"96","author":[{"given":"Catherine K.","family":"Smith","sequence":"first","affiliation":[{"name":"Department of Biology and Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139"}]},{"given":"Tania A.","family":"Baker","sequence":"additional","affiliation":[{"name":"Department of Biology and Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139"}]},{"given":"Robert T.","family":"Sauer","sequence":"additional","affiliation":[]}],"member":"341","published-online":{"date-parts":[[1999,6,8]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.genet.30.1.465"},{"key":"e_1_3_3_2_2","first-page":"57","volume":"77","author":"Sherman M Y","year":"1996","unstructured":"M Y Sherman, A L Goldberg EXS 77, 57\u201378 (1996).","journal-title":"EXS"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.1996.421404.x"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80431-6"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.94.12.6070"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1038\/nsb0297-133"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1995.0400"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1006\/jsbi.1998.4039"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.95.21.12135"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.91.25.12218"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1101\/gad.9.19.2399"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1002\/j.1460-2075.1995.tb07179.x"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.94.26.14378"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1101\/gad.11.7.815"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1101\/gad.12.24.3889"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1101\/gad.12.9.1338"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1101\/gad.12.9.1348"},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.179.23.7219-7225.1997"},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.92.8.3516"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.1002\/j.1460-2075.1995.tb07253.x"},{"key":"e_1_3_3_21_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.1999.01155.x"},{"key":"e_1_3_3_22_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80485-7"},{"key":"e_1_3_3_23_2","doi-asserted-by":"publisher","DOI":"10.1101\/gad.11.12.1561"},{"key":"e_1_3_3_24_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0968-0004(96)10038-4"},{"key":"e_1_3_3_25_2","doi-asserted-by":"publisher","DOI":"10.1101\/gr.9.1.27"},{"key":"e_1_3_3_26_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80417-1"},{"key":"e_1_3_3_27_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)81593-7"},{"key":"e_1_3_3_28_2","doi-asserted-by":"publisher","DOI":"10.1038\/1843"},{"key":"e_1_3_3_29_2","doi-asserted-by":"publisher","DOI":"10.1038\/nsb0894-518"},{"key":"e_1_3_3_30_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.271.5251.990"},{"key":"e_1_3_3_31_2","doi-asserted-by":"publisher","DOI":"10.1002\/pro.5560021219"},{"key":"e_1_3_3_32_2","first-page":"90","volume-title":"Analytical Ultracentrifugation in Biochemistry and Polymer Science","author":"Laue T M","year":"1992","unstructured":"T M Laue, B D Shah, T M Ridgeway, S L Pelletier Analytical Ultracentrifugation in Biochemistry and Polymer Science, eds S E Harding, A J Rowe, J C Hortons (R. 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