{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,16]],"date-time":"2025-10-16T20:02:58Z","timestamp":1760644978729},"reference-count":20,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2005,3,3]],"date-time":"2005-03-03T00:00:00Z","timestamp":1109808000000},"content-version":"vor","delay-in-days":11659,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["European Journal of Biochemistry"],"published-print":{"date-parts":[[1973,4]]},"abstract":"<jats:p>2\u2010Thiocytidine (s<jats:sup>2<\/jats:sup>C) is incorporated into yeast tRNA<jats:sup>phe<\/jats:sup>\u2010A<jats:sub>73<\/jats:sub>\u2010C<jats:sub>74<\/jats:sub> by tRNA nucleotidyl transferase. This leads to the formation of tRNA<jats:sup>Phe<\/jats:sup>\u2010A<jats:sub>73<\/jats:sub>\u2010C<jats:sub>74<\/jats:sub>\u2010s<jats:sup>2<\/jats:sup>C<jats:sub>75<\/jats:sub>, which can be further converted to tRNA<jats:sup>Phe<\/jats:sup>\u2010A<jats:sub>73<\/jats:sub>\u2010C<jats:sub>74<\/jats:sub>\u2010s<jats:sup>2<\/jats:sup>C<jats:sub>75<\/jats:sub>\u2010A<jats:sub>76<\/jats:sub>. tRNA<jats:sup>Phe<\/jats:sup> with the s<jats:sup>2<\/jats:sup>CMP\u2010containing 3\u2032\u2010end can be aminoacylated with the corresponding synthetase, exhibiting the same <jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub>\u2010values and slightly lowered <jats:italic>V<\/jats:italic> compared with tRNA<jats:sup>Phe<\/jats:sup>\u2010A<jats:sub>73<\/jats:sub>\u2010C<jats:sub>74<\/jats:sub>\u2010C<jats:sub>75<\/jats:sub>\u2010A<jats:sub>76<\/jats:sub>. The s<jats:sup>2<\/jats:sup>CMP incorporated is a specific site for binding <jats:italic>p<\/jats:italic>\u2010hydroxymercuribenzoate; formation of 1:1 complex with a dissociation constant <jats:italic>K<\/jats:italic><jats:sub>d<\/jats:sub>= 8.7 \u03bcM was observed. 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