Literature DB >> 19636968

1H, 13C and 15N resonance assignments of RNA pyrophosphohydrolase RppH from Escherichia coli.

Yunchen Bi1, Hongwei Li, Shoujin Fan, Bin Xia, Changwen Jin.   

Abstract

The mRNA degradation is an important regulatory mechanism which controls gene expression by limiting the number of translation times. Previous studies demonstrated that this process is essential for organisms. Escherichia coli RNA pyrophosphohydrolase (RppH) is an enzyme that triggers mRNA degradation by removing the 5' pyrophosphate, which is a rate-determining step. In order to understand the molecular mechanism of the biological function, the structural information of RppH is required. Herein, we report the resonance assignments of (1)H, (15)N, (13)C atoms of the E. coli RppH.

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Year:  2009        PMID: 19636968     DOI: 10.1007/s12104-009-9162-8

Source DB:  PubMed          Journal:  Biomol NMR Assign        ISSN: 1874-270X            Impact factor:   0.746


  2 in total

1.  Specificity and evolutionary conservation of the Escherichia coli RNA pyrophosphohydrolase RppH.

Authors:  Patricia L Foley; Ping-kun Hsieh; Daniel J Luciano; Joel G Belasco
Journal:  J Biol Chem       Date:  2015-02-05       Impact factor: 5.157

2.  Structures of RNA complexes with the Escherichia coli RNA pyrophosphohydrolase RppH unveil the basis for specific 5'-end-dependent mRNA decay.

Authors:  Nikita Vasilyev; Alexander Serganov
Journal:  J Biol Chem       Date:  2015-02-05       Impact factor: 5.157

  2 in total

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