{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T12:03:51Z","timestamp":1791115431167,"version":"4.1.0"},"reference-count":22,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2008,12,31]],"date-time":"2008-12-31T00:00:00Z","timestamp":1230681600000},"content-version":"vor","delay-in-days":4017,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000183","name":"Army Research Office","doi-asserted-by":"publisher","award":["DAAH04\u201094\u2010G\u20100335"],"award-info":[{"award-number":["DAAH04\u201094\u2010G\u20100335"]}],"id":[{"id":"10.13039\/100000183","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[1998,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>A subset of eukaryotic aminoacyl\u2010tRNA synthetases (a\u2010RS) are contained in a multienzyme complex for which little structural detail is known. Three reversible chemical crosslinking reagents have been used to investigate the arrangement of polypeptides within this particle as isolated from rabbit reticulocytes. Identification of the crosslinked protein pairs was accomplished by two\u2010dimensional SDS diagonal gel electrophoresis. Seventeen neighboring protein pairs have been identified. Eight are seen with at least two reagents: K\u2010RS:p38, D\u2010RS:K\u2010RS, R\u2010RS dimer, K\u2010RS dimer, K\u2010RS:Q\u2010RS, E\/P\u2010RS:K\u2010RS, E\/P\u2010RS:I\u2010RS, and Q\u2010RS with one of the nonsynthetase proteins. Nine more are observed with one reagent: D\u2010RS dimer, R\u2010RS:p43, D\u2010RS:Q\u2010RS, D\u2010RS:M\u2010RS, K\u2010RS:L\u2010RS, I\u2010RS:R\u2010RS, D\u2010RS:E\/P\u2010RS, I\u2010RS:Q\u2010RS, I\u2010RS:L\u2010RS. One trimeric association is seen: E\/P\u2010RS:I\u2010RS:L\u2010RS.<\/jats:p>\n                  <jats:p>The observed neighboring protein pairs suggest that the polypeptides within the aminoacyl\u2010tRNA synthetase complex are distributed in three structural domains of similar mass. These can be arranged in a U\u2010shaped particle in which each \u201carm\u201d is considered a domain and the third forms the \u201cbase\u201d of the structure. The arms have been termed domain I (D\u2010RS, M\u2010RS, Q\u2010RS) and domain II (K\u2010RS, R\u2010RS), with domain III (E\/P\u2010RS, I\u2010RS, L\u2010RS) assigned to the base. The smaller proteins (p38, p43) may bridge the domains. This proposed spatial relationship of these domains, as well as their compositions, are consistent with earlier studies. Thus, this study provides an initial three\u2010dimensional working model of the arrangement of polypeptides within the multienzyme aminoacyl\u2010tRNA synthetase complex.<\/jats:p>","DOI":"10.1002\/pro.5560070108","type":"journal-article","created":{"date-parts":[[2010,7,12]],"date-time":"2010-07-12T03:16:17Z","timestamp":1278904577000},"page":"79-87","source":"Crossref","is-referenced-by-count":46,"title":["Structural analysis of the multienzyme aminoacyl\u2010tRNA synthetase complex: A three\u2010domain model based on reversible chemical crosslinking"],"prefix":"10.1002","volume":"7","author":[{"given":"Mona T.","family":"Norcum","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J. 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