• Search Research Projects
  • Search Researchers
  • How to Use
  1. Back to previous page

In Vivo Function of tRNase Z in Esherichia coli and Yeast Saccharomyces cerevisiae

Research Project

Project/Area Number 20780063
Research Category

Grant-in-Aid for Young Scientists (B)

Allocation TypeSingle-year Grants
Research Field Applied microbiology
Research InstitutionNigata University of Phermacy and Applied Life Sciences

Principal Investigator

TAKAKU Hiroaki  Nigata University of Phermacy and Applied Life Sciences, 応用生命科学部, 准教授 (70350717)

Co-Investigator(Renkei-kenkyūsha) NASHIMOTO Masayuki  新潟薬科大学, 応用生命科学部, 教授 (30228069)
TAKAGI Masamichi  新潟薬科大学, 学長 (50018339)
Project Period (FY) 2008 – 2009
Project Status Completed (Fiscal Year 2009)
Budget Amount *help
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2009: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2008: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Keywords微生物酵素 / tRNaseZ / 前駆体tRNA / 酵母 / tRNAの3'プロセシング / エンド型リボヌクレアーゼ / tRNase Z / 成熟tRNA / 大腸菌 / アミノアシルtRNA
Research Abstract

In most organisms, tRNase Z is thought to be essential for 3′ processing of tRNA molecules. The Escherichia coli tRNase ZS gene, however, appears to be dispensable under normal growth conditions. Here we intensively examined various (pre-)tRNAs for good substrates of E. coli tRNase ZS in vitro, and found that the enzyme can nibble off the 3′ terminal CCA residues from mature tRNAs. Furthermore, we discovered that E. coli tRNase ZS, when sufficiently expressed in the cell, shuts down growth by removing amino acids from aminoacyl-tRNAs. The current data suggest that tRNase ZS may help modulate a cell growth rate by repressing translation under some stressful conditions. We also examined 3′ processing activity of recombinant yeast tRNase ZL against various yeast pre-tRNAs in vitro. The recombinant yeast tRNase ZL was able to cleavage yeast pre-tRNAs efficiently after the discriminator nucleotide. Taken together, we speculate the difference of tRNase Z domain structure between E. coli and yeast might lead to the specificity of substrate recognition and cleavage site.

Report

(3 results)
  • 2009 Annual Research Report   Final Research Report ( PDF )
  • 2008 Annual Research Report
  • Research Products

    (2 results)

All 2008

All Journal Article (2 results) (of which Peer Reviewed: 2 results)

  • [Journal Article] Escherichia coli tRNase Z can shut down growth probably by removing amino acids from aminoacyl-tRNAs.2008

    • Author(s)
      Takaku H, Nashimoto M.
    • Journal Title

      Genes Cells 13(11)

      Pages: 1087-97

    • Related Report
      2009 Final Research Report
    • Peer Reviewed
  • [Journal Article] Escherichia coli tRNase Z can shut down growth probably by removine amino acids from aminoacvl-tRNAs2008

    • Author(s)
      Takaku H, Nashimoto M
    • Journal Title

      Genes to Cells 11

      Pages: 1087-1097

    • Related Report
      2008 Annual Research Report
    • Peer Reviewed

URL: 

Published: 2008-04-01   Modified: 2016-04-21  

Information User Guide FAQ News Terms of Use Attribution of KAKENHI

Powered by NII kakenhi