Literature DB >> 7599277

tRNA-m1G methyltransferase interactions: touching bases with structure.

W M Holmes1, C Andraos-Selim, M Redlak.   

Abstract

m1G methyltransferase of Escherichia coli is being examined with regard to how specific tRNA substrates are recognized. This enzyme appears to require the entire tRNA structure of optimal activity. Recognition may require specific base contacts as well as phosphate backbone structures embodied in the tRNA structure.

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Year:  1995        PMID: 7599277     DOI: 10.1016/0300-9084(96)88105-3

Source DB:  PubMed          Journal:  Biochimie        ISSN: 0300-9084            Impact factor:   4.079


  3 in total

1.  Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition.

Authors:  Hyung Jun Ahn; Hyeon-Woo Kim; Hye-Jin Yoon; Byung Il Lee; Se Won Suh; Jin Kuk Yang
Journal:  EMBO J       Date:  2003-06-02       Impact factor: 11.598

2.  Characterization of Streptococcus pneumoniae TrmD, a tRNA methyltransferase essential for growth.

Authors:  Karen O'Dwyer; Joseph M Watts; Sanjoy Biswas; Jennifer Ambrad; Michael Barber; Hervé Brulé; Chantal Petit; David J Holmes; Magdalena Zalacain; Walter M Holmes
Journal:  J Bacteriol       Date:  2004-04       Impact factor: 3.490

3.  Identification of determinants for tRNA substrate recognition by Escherichia coli C/U34 2'-O-methyltransferase.

Authors:  Mi Zhou; Tao Long; Zhi-Peng Fang; Xiao-Long Zhou; Ru-Juan Liu; En-Duo Wang
Journal:  RNA Biol       Date:  2015       Impact factor: 4.652

  3 in total

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