Identification and sequence analysis of metazoan tRNA 3'-end processing enzymes tRNase Zs

PLoS One. 2012;7(9):e44264. doi: 10.1371/journal.pone.0044264. Epub 2012 Sep 4.

Abstract

tRNase Z is the endonuclease responsible for removing the 3'-trailer sequences from precursor tRNAs, a prerequisite for the addition of the CCA sequence. It occurs in the short (tRNase Z(S)) and long (tRNase Z(L)) forms. Here we report the identification and sequence analysis of candidate tRNase Zs from 81 metazoan species. We found that the vast majority of deuterostomes, lophotrochozoans and lower metazoans have one tRNase Z(S) and one tRNase Z(L) genes, whereas ecdysozoans possess only a single tRNase Z(L) gene. Sequence analysis revealed that in metazoans, a single nuclear tRNase Z(L) gene is likely to encode both the nuclear and mitochondrial forms of tRNA 3'-end processing enzyme through mechanisms that include alternative translation initiation from two in-frame start codons and alternative splicing. Sequence conservation analysis revealed a variant PxKxRN motif, PxPxRG, which is located in the N-terminal region of tRNase Z(S)s. We also identified a previously unappreciated motif, AxDx, present in the C-terminal region of both tRNase Z(S)s and tRNase Z(L)s. The AxDx motif consisting mainly of a very short loop is potentially close enough to form hydrogen bonds with the loop containing the PxKxRN or PxPxRG motif. Through complementation analysis, we demonstrated the likely functional importance of the AxDx motif. In conclusion, our analysis supports the notion that in metazoans a single tRNase Z(L) has evolved to participate in both nuclear and mitochondrial tRNA 3'-end processing, whereas tRNase Z(S) may have evolved new functions. Our analysis also unveils new evolutionarily conserved motifs in tRNase Zs, including the C-terminal AxDx motif, which may have functional significance.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alternative Splicing
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Cell Nucleus / enzymology*
  • Cell Nucleus / genetics
  • Endoribonucleases / chemistry*
  • Endoribonucleases / genetics
  • Endoribonucleases / metabolism
  • Humans
  • Isoenzymes / chemistry
  • Isoenzymes / genetics
  • Isoenzymes / metabolism
  • Mitochondria / enzymology*
  • Mitochondria / genetics
  • Molecular Sequence Data
  • Phylogeny
  • Protein Structure, Tertiary
  • RNA 3' End Processing*
  • RNA Precursors / metabolism
  • RNA, Transfer / metabolism*
  • Sequence Alignment
  • Sequence Analysis, Protein

Substances

  • Isoenzymes
  • RNA Precursors
  • RNA, Transfer
  • Endoribonucleases
  • tRNase Z, human

Grants and funding

This work was supported in part by grants from the National Science Foundation of China (31070703) (http://www.nsfc.gov.cn/Portal0/default152.htm) and the Priority Academic Program Development of Jiangsu Higher Education Institutions (http://jsycw.ec.js.edu.cn/) and Nanjing Normal University (2007104XGQ0148). The funders had no role in study design, data colletion and analysis, decision to publish, or preparation of the manuscript.