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5.4.99.B22
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study of the oligomerisation in solution of purified recombinant yeast tRNA:pseudouridine synthetase Pus1 in the presence or absence oftRNA. The presence of the neutral detergent dodecyl-beta-D-maltoside helps in avoiding the oligomerization/inactivation of the purified Pus1 in the absence of tRNA
648856
5.4.99.B22
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the hPus1p enzyme binds to its RNA substrate as a monomer. The C-terminal end of hPus1p folds into two alpha-helices and these helices pack against the back of the hPus1p molecule, which prevents the dimerization observed in the bacterial homologue, TruA. This C-terminal region is responsible for the atypical RNA substrate binding and activity of hPus1p. Enzyme crystal structure analysis, overview
749148
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