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J. Biol. Chem., Vol. 263, Issue 5, 2255-2263, Feb, 1988
HO Kammen, CC Marvel, L Hardy and EE Penhoet
The RNA modification enzyme, tRNA pseudouridine synthase I has been
isolated in 95% purity from an Escherichia coli strain harboring a
multicopy plasmid with a 2.3-kilobase pair insert from the hisT operon. Its
molecular size, amino acid composition, and amino-terminal sequence
correspond to those predicted by the structure and expression of the hisT
gene. Enzyme activity, as measured by a 3H release assay, is unaffected by
pretreatment of tRNA pseudouridine synthase I with micrococcal nuclease and
is optimized by the addition of a monovalent cation and thiol reductant.
The activity is inhibited by all tRNA species tested, including substrates,
modified tRNAs, nonsubstrates, or tRNAs containing 5-fluorouridine. Binding
of tRNA pseudouridine synthase I occurs with both substrate and
nonsubstrate tRNAs and does not require a monovalent cation. Our findings
are consistent with a multistep mechanism whereby tRNA pseudouridine
synthase I first binds nonspecifically and then forms transient covalent
adducts with tRNA substrates. In the absence of other proteins, purified
tRNA pseudouridine synthase I forms psi at all three modification sites
known to be affected in hisT mutants. The 36.4-kDa polypeptide product of
the gene adjacent to hisT, whose translation is linked to that of tRNA
pseudouridine synthase I, is not a functional subunit for tRNA
pseudouridine synthase I activity, nor is it a separate synthase acting at
one of the three loci.
Purification, structure, and properties of Escherichia coli tRNA pseudouridine synthase I
Naval Biosciences Laboratory, University of California, Berkeley 94720.
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