Literature DB >> 12234679

G350 of Escherichia coli RNase P RNA contributes to Mg2+ binding near the active site of the enzyme.

Terri A Rasmussen1, James M Nolan.   

Abstract

G350 of Escherichia coli RNase P RNA is a highly conserved residue among all bacteria and lies near the known magnesium binding site for the RNase P ribozyme, helix P4. Mutations at G350 have a dramatic effect on substrate cleavage activity for both RNA alone and holoenzyme; the G350C mutation has the most severe phenotype. The G350C mutation also inhibits growth of cells that express the mutant RNA in vivo under conditions of magnesium starvation. The results suggest that G350 contributes to Mg(2+) binding at helix P4 of RNase P RNA.

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Year:  2002        PMID: 12234679     DOI: 10.1016/s0378-1119(02)00766-7

Source DB:  PubMed          Journal:  Gene        ISSN: 0378-1119            Impact factor:   3.688


  4 in total

1.  Microenvironment analysis and identification of magnesium binding sites in RNA.

Authors:  D Rey Banatao; Russ B Altman; Teri E Klein
Journal:  Nucleic Acids Res       Date:  2003-08-01       Impact factor: 16.971

2.  Crystal structure of a bacterial ribonuclease P RNA.

Authors:  Alexei V Kazantsev; Angelika A Krivenko; Daniel J Harrington; Stephen R Holbrook; Paul D Adams; Norman R Pace
Journal:  Proc Natl Acad Sci U S A       Date:  2005-09-12       Impact factor: 11.205

3.  NMR and XAS reveal an inner-sphere metal binding site in the P4 helix of the metallo-ribozyme ribonuclease P.

Authors:  Kristin S Koutmou; Anette Casiano-Negroni; Melissa M Getz; Samuel Pazicni; Andrew J Andrews; James E Penner-Hahn; Hashim M Al-Hashimi; Carol A Fierke
Journal:  Proc Natl Acad Sci U S A       Date:  2010-01-25       Impact factor: 11.205

4.  Hybrid E. coli--Mitochondrial ribonuclease P RNAs are catalytically active.

Authors:  Elias Seif; Alexandre Cadieux; B Franz Lang
Journal:  RNA       Date:  2006-08-07       Impact factor: 4.942

  4 in total

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