Mechanism for the alteration of the substrate specificities of template-independent RNA polymerases

Yukimatsu Toh, Daijiro Takeshita, Takashi Nagaike, Tomoyuki Numata, Kozo Tomita

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)

Abstract

PolyA polymerase (PAP) adds a polyA tail onto the 3′-end of RNAs without a nucleic acid template, using adenosine-5′-triphosphate (ATP) as a substrate. The mechanism for the substrate selection by eubacterial PAP remains obscure. Structural and biochemical studies of Escherichia coli PAP (EcPAP) revealed that the shape and size of the nucleobase-interacting pocket of EcPAP are maintained by an intra-molecular hydrogen-network, making it suitable for the accommodation of only ATP, using a single amino acid, Arg 197. The pocket structure is sustained by interactions between the catalytic domain and the RNA-binding domain. EcPAP has a flexible basic C-terminal region that contributes to optimal RNA translocation for processive adenosine 5′-monophosphate (AMP) incorporations onto the 3′-end of RNAs. A comparison of the EcPAP structure with those of other template-independent RNA polymerases suggests that structural changes of domain(s) outside the conserved catalytic core domain altered the substrate specificities of the template-independent RNA polymerases.

Original languageEnglish
Pages (from-to)232-243
Number of pages12
JournalStructure
Volume19
Issue number2
DOIs
Publication statusPublished - Feb 9 2011

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

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