How the CCA-Adding Enzyme Selects Adenine over Cytosine at Position 76 of tRNA

Author:

Pan Baocheng1,Xiong Yong1,Steitz Thomas A.123

Affiliation:

1. Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.

2. Department of Chemistry, Yale University, New Haven, CT 06520, USA.

3. Howard Hughes Medical Institute, New Haven, CT 06520, USA.

Abstract

Adding CCA Translation of a gene sequence into protein is mediated by transfer RNA (tRNA), which has a specific cytosine-adenine (CCA) tail to which amino acids attach and is recognized by enzymes. The tail, however, does not have a DNA template, and instead CCA-adding enzymes bolt on the additional nucleosides. Crystal structures have shown how these enzymes achieve specificity for cytosine, but we did not know how they select the final adenine until Pan et al. (p. 937 ) described CCA-adding enzyme structures captured at several stages of the reaction. Crystallized enzymes were complexed with a tRNA mimic and the respective cytosine or adenine triphosphate. The final adenine was discovered to be incorporated by the mediation of a single Mg 2+ ion in the enzyme, but no more cytosine could be attached because its triphosphate could not then get into the right position for the reaction.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference24 articles.

1. tRNA nucleotidyltransferase;Deutscher M. P.;The Enzymes,1982

2. CCA-adding enzymes and poly(A) polymerases are all members of the same nucleotidyltransferase superfamily: Characterization of the CCA-adding enzyme from the archaeal hyperthermophile Sulfolobus shibatae;Yue D.;RNA,1996

3. Crystal Structures of an Archaeal Class I CCA-Adding Enzyme and Its Nucleotide Complexes

4. Divergent evolutions of trinucleotide polymerization revealed by an archaeal CCA-adding enzyme structure

5. Mechanism of transfer RNA maturation by CCA-adding enzyme without using an oligonucleotide template

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