{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,20]],"date-time":"2026-01-20T00:33:21Z","timestamp":1768869201257,"version":"3.49.0"},"reference-count":49,"publisher":"Portland Press Ltd.","issue":"6","license":[{"start":{"date-parts":[[2019,7,25]],"date-time":"2019-07-25T00:00:00Z","timestamp":1564012800000},"content-version":"vor","delay-in-days":2474,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/2.5\/"}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2012,12,1]]},"abstract":"<jats:p>A putative protease gene (tldD) was previously identified from studying tolerance of letD encoding the CcdB toxin of a toxin\u2013antidote system of the F plasmid in Escherichia coli. While this gene is evolutionarily conserved in archaea and bacteria, the proteolytic activity of encoded proteins remained to be demonstrated experimentally. Here we studied Sso0660, an archaeal TldD homologue encoded in Sulfolobus solfataricus by overexpression of the recombinant protein and characterization of the purified enzyme. We found that the enzyme is active in degrading azocasein and FITC\u2013BSA substrates. Protease inhibitor studies showed that EDTA and o-phenanthroline, two well-known metalloprotease inhibitors, either abolished completely or strongly inhibited the enzyme activity, and flame spectrometric analysis showed that a zinc ion is a cofactor of the protease. Furthermore, the protein forms disulfide bond via the Cys416 residue, yielding protein dimer that is the active form of the enzyme. These results establish for the first time that tidD genes encode zinc-containing proteases, classifying them as a family in the metalloprotease class.<\/jats:p>","DOI":"10.1042\/bsr20120074","type":"journal-article","created":{"date-parts":[[2012,9,6]],"date-time":"2012-09-06T08:10:39Z","timestamp":1346919039000},"page":"609-618","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["An archaeal protein evolutionarily conserved in prokaryotes is a zinc-dependent metalloprotease"],"prefix":"10.1042","volume":"32","author":[{"given":"Yongmei","family":"Hu","sequence":"first","affiliation":[{"name":"State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nan","family":"Peng","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wenyuan","family":"Han","sequence":"additional","affiliation":[{"name":"Archaeal Centre, Department of Biology, University of Copenhagen, Ole Maal\u00f8es Vej 5, Copenhagen Biocenter, DK-2200 Copenhagen N, Denmark"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yuxia","family":"Mei","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zhengjun","family":"Chen","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xu","family":"Feng","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yun\u00a0Xiang","family":"Liang","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Qunxin","family":"She","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China"},{"name":"Archaeal Centre, Department of Biology, University of Copenhagen, Ole Maal\u00f8es Vej 5, Copenhagen Biocenter, DK-2200 Copenhagen N, Denmark"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2012,10,15]]},"reference":[{"key":"2021111618133821300_B1","doi-asserted-by":"crossref","first-page":"D343","DOI":"10.1093\/nar\/gkr987","article-title":"MEROPS: the database of proteolytic enzymes, their substrates and inhibitors","volume":"40","author":"Rawlings","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"2021111618133821300_B2","doi-asserted-by":"crossref","first-page":"7835","DOI":"10.1073\/pnas.141222098","article-title":"The complete genome of the crenarchaeon Sulfolobus solfataricus P2","volume":"98","author":"She","year":"2001","journal-title":"Proc. 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