BMC Biochemistry

Featured article: An evolutionary encounter between tRNA and myelin maturation

tRNA splicing is an essential process in the maturation of eukaryotic pre-tRNA molecules. This study shows that tRNA healing enzymes from yeast and lancelet share structural and functional properties with members of the 2H-phosphoesterase superfamily, in particular the vertebrate myelin enzyme CNPase. While domain organization has been conserved, functions of the individual domains may have been altered or lost during evolution.

The conserved residues of Dnmt3a, R200 and R202, are essential for methylation activity. They are involved in positioning of the flipped target base and in creating and stabilizing of the transient covalent intermediate of the methylation reaction.

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Aims and scope

BMC Biochemistry is an open access, peer-reviewed journal that considers articles on all aspects of biochemical processes, including the structure, function and dynamics of metabolic pathways, supramolecular complexes, enzymes, proteins, nucleic acids and small molecular components of organelles, cells and tissues.

Editor

Alexandros Houssein, BioMed Central

Section Editors

Sabato D'Auria, CNR
Chris Grant, University of Manchester
Albert Jeltsch, Universität Stuttgart
Joel Weiner, University of Alberta

Joel Weiner, Section Editor

Dr. Joel Weiner is a Emeritus Distinguished University Professor of Biochemistry and Medical Microbiology & Immunology at the University of Alberta. Dr. Weiner’s research focuses on the function and structure of membrane-bound energy conserving enzymes with emphasis on molybdoenzymes and flavoenzymes. He joined the editorial board of BMC Biochemistry in 2010.

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